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TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)

 TRAF6_MOUSE             Reviewed;         530 AA.
P70196; Q6P9M0; Q8BLV2;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 2.
27-SEP-2017, entry version 180.
RecName: Full=TNF receptor-associated factor 6;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase TRAF6;
AltName: Full=RING-type E3 ubiquitin transferase TRAF6 {ECO:0000305};
Name=Traf6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/Kaplan; TISSUE=T-cell lymphoma;
PubMed=8910514; DOI=10.1074/jbc.271.46.28745;
Ishida T., Mizushima S., Azuma S., Kobayashi N., Tojo T., Suzuki K.,
Aizawa S., Watanabe T., Mosialos G., Kieff E., Yamamoto T., Inoue J.;
"Identification of TRAF6, a novel tumor necrosis factor receptor-
associated factor protein that mediates signaling from an amino-
terminal domain of the CD40 cytoplasmic region.";
J. Biol. Chem. 271:28745-28748(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10421844; DOI=10.1046/j.1365-2443.1999.00265.x;
Naito A., Azuma S., Tanaka S., Miyazaki T., Takaki S., Takatsu K.,
Nakao K., Nakamura K., Katsuki M., Yamamoto T., Inoue J.;
"Severe osteopetrosis, defective interleukin-1 signalling and lymph
node organogenesis in TRAF6-deficient mice.";
Genes Cells 4:353-362(1999).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10215628; DOI=10.1101/gad.13.8.1015;
Lomaga M.A., Yeh W.C., Sarosi I., Duncan G.S., Furlonger C., Ho A.,
Morony S., Capparelli C., Van G., Kaufman S., van der Heiden A.,
Itie A., Wakeham A., Khoo W., Sasaki T., Cao Z., Penninger J.M.,
Paige C.J., Lacey D.L., Dunstan C.R., Boyle W.J., Goeddel D.V.,
Mak T.W.;
"TRAF6 deficiency results in osteopetrosis and defective interleukin-
1, CD40, and LPS signaling.";
Genes Dev. 13:1015-1024(1999).
[7]
INTERACTION WITH SQSTM1 AND PRKCZ.
PubMed=10747026; DOI=10.1093/emboj/19.7.1576;
Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.;
"The atypical PKC-interacting protein p62 channels NF-kappaB
activation by the IL-1-TRAF6 pathway.";
EMBO J. 19:1576-1586(2000).
[8]
INTERACTION WITH IL17R.
PubMed=10748240; DOI=10.1084/jem.191.7.1233;
Schwandner R., Yamaguchi K., Cao Z.;
"Requirement of tumor necrosis factor receptor-associated factor
(TRAF)6 in interleukin 17 signal transduction.";
J. Exp. Med. 191:1233-1240(2000).
[9]
INTERACTION WITH SQSTM1; PRKCZ AND NGFR.
PubMed=11244088; DOI=10.1074/jbc.C000869200;
Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T.,
Barker P.A., Moscat J.;
"The atypical protein kinase C-interacting protein p62 is a scaffold
for NF-kappaB activation by nerve growth factor.";
J. Biol. Chem. 276:7709-7712(2001).
[10]
DISRUPTION PHENOTYPE.
PubMed=12060722; DOI=10.1073/pnas.132636999;
Naito A., Yoshida H., Nishioka E., Satoh M., Azuma S., Yamamoto T.,
Nishikawa S., Inoue J.;
"TRAF6-deficient mice display hypohidrotic ectodermal dysplasia.";
Proc. Natl. Acad. Sci. U.S.A. 99:8766-8771(2002).
[11]
FUNCTION, AND INTERACTION WITH CD40 AND MAP3K8.
PubMed=12881420; DOI=10.1093/emboj/cdg386;
Eliopoulos A.G., Wang C.C., Dumitru C.D., Tsichlis P.N.;
"Tpl2 transduces CD40 and TNF signals that activate ERK and regulates
IgE induction by CD40.";
EMBO J. 22:3855-3864(2003).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=14499111; DOI=10.1016/S1074-7613(03)00230-9;
Kobayashi T., Walsh P.T., Walsh M.C., Speirs K.M., Chiffoleau E.,
King C.G., Hancock W.W., Caamano J.H., Hunter C.A., Scott P.,
Turka L.A., Choi Y.;
"TRAF6 is a critical factor for dendritic cell maturation and
development.";
Immunity 19:353-363(2003).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15322147; DOI=10.4049/jimmunol.173.5.2913;
Gohda J., Matsumura T., Inoue J.;
"TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent
pathway but not toll/IL-1 receptor domain-containing adaptor-inducing
IFN-beta (TRIF)-dependent pathway in TLR signaling.";
J. Immunol. 173:2913-2917(2004).
[14]
UBIQUITINATION.
PubMed=16079148; DOI=10.1074/jbc.C500237200;
Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T.,
Moscat J.;
"The p62 scaffold regulates nerve growth factor-induced NF-kappaB
activation by influencing TRAF6 polyubiquitination.";
J. Biol. Chem. 280:35625-35629(2005).
[15]
DISRUPTION PHENOTYPE.
PubMed=15705807; DOI=10.1126/science.1105677;
Akiyama T., Maeda S., Yamane S., Ogino K., Kasai M., Kajiura F.,
Matsumoto M., Inoue J.;
"Dependence of self-tolerance on TRAF6-directed development of thymic
stroma.";
Science 308:248-251(2005).
[16]
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).
[17]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17633018;
Inoue J., Gohda J., Akiyama T.;
"Characteristics and biological functions of TRAF6.";
Adv. Exp. Med. Biol. 597:72-79(2007).
[18]
FUNCTION, AND INTERACTION WITH LIMD1.
PubMed=17092936; DOI=10.1074/jbc.M607399200;
Feng Y., Zhao H., Luderer H.F., Epple H., Faccio R., Ross F.P.,
Teitelbaum S.L., Longmore G.D.;
"The LIM protein, Limd1, regulates AP-1 activation through an
interaction with Traf6 to influence osteoclast development.";
J. Biol. Chem. 282:39-48(2007).
[19]
INTERACTION WITH TRAFD1.
PubMed=18849341; DOI=10.1074/jbc.M806923200;
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
Yoshimura A.;
"FLN29 deficiency reveals its negative regulatory role in the Toll-
like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
helicase signaling pathway.";
J. Biol. Chem. 283:33858-33864(2008).
[20]
INTERACTION WITH RSAD2, AND SUBCELLULAR LOCATION.
PubMed=21435586; DOI=10.1016/j.immuni.2011.03.010;
Saitoh T., Satoh T., Yamamoto N., Uematsu S., Takeuchi O., Kawai T.,
Akira S.;
"Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-
like receptor 9-mediated type I interferon production in plasmacytoid
dendritic cells.";
Immunity 34:352-363(2011).
-!- 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 (By
similarity). 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:0000250|UniProtKB:Q9Y4K3,
ECO:0000269|PubMed:10215628, ECO:0000269|PubMed:10421844,
ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:14499111,
ECO:0000269|PubMed:15322147, ECO:0000269|PubMed:17092936,
ECO:0000269|PubMed:17633018}.
-!- 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 (By similarity). Homooligomer (By similarity).
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 (By similarity). Associates with
NGFR, TNFRSF17, IRAK2, IRAK3, PELI2, PELI3, RIPK2, MAP3K1, MAP3K5,
MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor
associated protein TDP2. Binds UBE2V1. Interacts with MAVS/IPS1.
Interacts with TAX1BP1 (By similarity). Interacts with IL17R.
Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary
complex with SQSTM1 and PRKCZ. Interacts with IL1RL1. Interacts
with AJUBA (By similarity). Interacts with TRAFD1. Interacts with
TICAM2. Interacts with ZFAND5. Interacts with ARRB1 and ARRB2 (By
similarity). 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) (By similarity). Interacts
(via TRAF domains) with WDR34 (via WD domains). Interacts with
RBCK1 (By similarity). Interacts with TRAF3IP2 (By similarity).
Interacts with LIMD1 (via LIM domains). Interacts with
RSAD2/viperin. Interacts with IFIT3 (via N-terminus) (By
similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the
kinase catalytic domain). Interacts with CARD14 (By similarity).
Interacts with CD40 and MAP3K8; the interaction is required for
ERK activation. Interacts with TICAM1 and this interaction is
enhanced in the presence of WDFY1 (By similarity). Interacts with
TANK; this interaction increases in response to DNA damage (By
similarity). Interacts with USP10; this interaction increases in
response to DNA damage (By similarity). Interacts with ZC3H12A;
this interaction increases in response to DNA damage and is
stimulated by TANK (By similarity). {ECO:0000250|UniProtKB:Q9Y4K3,
ECO:0000269|PubMed:10747026, ECO:0000269|PubMed:10748240,
ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12881420,
ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:17092936,
ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:21435586}.
-!- INTERACTION:
P27512:Cd40; NbExp=2; IntAct=EBI-448028, EBI-525742;
Q9QZH6:Ecsit; NbExp=4; IntAct=EBI-448028, EBI-527020;
Q9EQY0:Ern1; NbExp=6; IntAct=EBI-448028, EBI-5480799;
P17879:Hspa1b; NbExp=3; IntAct=EBI-448028, EBI-397360;
Q62406-1:Irak1; NbExp=4; IntAct=EBI-448028, EBI-488313;
Q8K4B2:Irak3; NbExp=3; IntAct=EBI-448028, EBI-646179;
Q61084:Map3k3; NbExp=5; IntAct=EBI-448028, EBI-446250;
Q62227:Nr0b2; NbExp=5; IntAct=EBI-448028, EBI-4310440;
P35235:Ptpn11; NbExp=2; IntAct=EBI-448028, EBI-397236;
Q793I8:Tifa; NbExp=2; IntAct=EBI-448028, EBI-524817;
O35305:Tnfrsf11a; NbExp=2; IntAct=EBI-448028, EBI-647362;
Q8C0E5:Traf3ip2; NbExp=3; IntAct=EBI-448028, EBI-530713;
Q8N7N6:Traf3ip2; NbExp=4; IntAct=EBI-448028, EBI-646165;
Q3UDK1:Trafd1; NbExp=2; IntAct=EBI-448028, EBI-1396948;
P62991:Ubc; NbExp=2; IntAct=EBI-448028, EBI-413074;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}.
Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus
{ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet
{ECO:0000269|PubMed:21435586}. Note=RSAD2/viperin recruits it to
the lipid droplet.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70196-1; Sequence=Displayed;
Name=2;
IsoId=P70196-2; Sequence=VSP_007404, VSP_007405;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, lung, liver,
skeletal muscle, and kidney; lower expression in heart, spleen,
and testis.
-!- 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-461 with SUMO1.
{ECO:0000250|UniProtKB:Q9Y4K3}.
-!- PTM: Polyubiquitinated; 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. {ECO:0000250|UniProtKB:Q9Y4K3}.
-!- DISRUPTION PHENOTYPE: Abrogation of IL-1-induced activation of NF-
kappa-B, MAPK8/JNK and MAPK14/p38. Animals appears normal at birth
but becomes smaller after one week. Show runting, failure of tooth
eruption and die after three weeks. Exhibit severe osteopetrosis,
thymic atrophy, lymph node deficiency, splenomegaly, and have
alopecia and lack sweat glands. {ECO:0000269|PubMed:10215628,
ECO:0000269|PubMed:10421844, ECO:0000269|PubMed:12060722,
ECO:0000269|PubMed:14499111, ECO:0000269|PubMed:15322147,
ECO:0000269|PubMed:15705807, ECO:0000269|PubMed:17633018}.
-!- SIMILARITY: Belongs to the TNF receptor-associated factor family.
A subfamily. {ECO:0000305}.
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EMBL; D84655; BAA12705.1; -; mRNA.
EMBL; AK041172; BAC30850.1; -; mRNA.
EMBL; AK155434; BAE33263.1; -; mRNA.
EMBL; AL929571; CAM20505.1; -; Genomic_DNA.
EMBL; CH466519; EDL27656.1; -; Genomic_DNA.
EMBL; CH466519; EDL27657.1; -; Genomic_DNA.
EMBL; BC060705; AAH60705.1; -; mRNA.
CCDS; CCDS16464.1; -. [P70196-1]
RefSeq; NP_001290202.1; NM_001303273.1. [P70196-1]
RefSeq; NP_033450.2; NM_009424.3. [P70196-1]
UniGene; Mm.292729; -.
ProteinModelPortal; P70196; -.
SMR; P70196; -.
BioGrid; 204307; 102.
CORUM; P70196; -.
DIP; DIP-29812N; -.
IntAct; P70196; 37.
MINT; MINT-252449; -.
STRING; 10090.ENSMUSP00000004949; -.
iPTMnet; P70196; -.
PhosphoSitePlus; P70196; -.
EPD; P70196; -.
MaxQB; P70196; -.
PaxDb; P70196; -.
PeptideAtlas; P70196; -.
PRIDE; P70196; -.
Ensembl; ENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164. [P70196-1]
GeneID; 22034; -.
KEGG; mmu:22034; -.
UCSC; uc008lhl.2; mouse. [P70196-2]
UCSC; uc008lhm.2; mouse. [P70196-1]
CTD; 7189; -.
MGI; MGI:108072; Traf6.
eggNOG; ENOG410ISDW; Eukaryota.
eggNOG; ENOG410XTXK; LUCA.
GeneTree; ENSGT00550000074359; -.
HOGENOM; HOG000006625; -.
HOVERGEN; HBG060248; -.
InParanoid; P70196; -.
KO; K03175; -.
OMA; PGYKLCL; -.
OrthoDB; EOG091G0GHD; -.
PhylomeDB; P70196; -.
TreeFam; TF321154; -.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
Reactome; R-MMU-209560; NF-kB is activated and signals survival.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-446652; Interleukin-1 family signaling.
Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
Reactome; R-MMU-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-MMU-937072; TRAF6 mediated induction of TAK1 complex.
Reactome; R-MMU-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-MMU-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-MMU-975155; MyD88 dependent cascade initiated on endosome.
Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
Reactome; R-MMU-975871; MyD88 cascade initiated on plasma membrane.
UniPathway; UPA00143; -.
PRO; PR:P70196; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027164; -.
CleanEx; MM_TRAF6; -.
Genevisible; P70196; MM.
GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; TAS:MGI.
GO; GO:0031996; F:thioesterase binding; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
GO; GO:0046849; P:bone remodeling; IMP:UniProtKB.
GO; GO:0045453; P:bone resorption; IMP:UniProtKB.
GO; GO:0048468; P:cell development; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0006955; P:immune response; IMP:MGI.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IMP:MGI.
GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IMP:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IDA:MGI.
GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
GO; GO:0042088; P:T-helper 1 type immune response; IMP:MGI.
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;
Alternative splicing; 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 1 530 TNF receptor-associated factor 6.
/FTId=PRO_0000056408.
DOMAIN 358 507 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 1 362 Interaction with TAX1BP1. {ECO:0000250}.
REGION 363 530 Interaction with TANK.
{ECO:0000250|UniProtKB:Q9Y4K3}.
COILED 299 356 {ECO:0000255}.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q9Y4K3}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 461 461 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 100 174 DAGHKCPVDNEILLENQLFPDNFAKREILSLTVKCPNKGCL
QKMELRHLEDHQVHCEFALVNCPQCQRPFQKCQV -> YLI
LRKHGALQQPNVKSMLETGHPKNRQTENTGQEHSRMDRNLR
QLGSHPSLYYGMNRGLLPCLPTQPPGKLQSP (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007404.
VAR_SEQ 175 530 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007405.
CONFLICT 251 251 E -> Q (in Ref. 1; BAA12705 and 2;
BAC30850). {ECO:0000305}.
CONFLICT 367 367 N -> K (in Ref. 1; BAA12705 and 2;
BAC30850). {ECO:0000305}.
SEQUENCE 530 AA; 60070 MW; F8389250425E4E2D CRC64;
MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM EEIQGYDVEF
DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD AGHKCPVDNE ILLENQLFPD
NFAKREILSL TVKCPNKGCL QKMELRHLED HQVHCEFALV NCPQCQRPFQ KCQVNTHIIE
DCPRRQVSCV NCAVSMAYEE KEIHDQSCPL ANIICEYCGT ILIREQMPNH YDLDCPTAPI
PCTFSVFGCH EKMQRNHLAR HLQENTQLHM RLLAQAVHNV NLALRPCDAA SPSRGCRPED
PNYEETIKQL ESRLVRQDHQ IRELTAKMET QSMYVGELKR TIRTLEDKVA EMEAQQCNGI
YIWKIGNFGM HLKSQEEERP VVIHSPGFYT GRPGYKLCMR LHLQLPTAQR CANYISLFVH
TMQGEYDSHL PWPFQGTIRL TILDQSEALI RQNHEEVMDA KPELLAFQRP TIPRNPKGFG
YVTFMHLEAL RQGTFIKDDT LLVRCEVSTR FDMGGLRKEG FQPRSTDAGV


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