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P70196 (TRAF6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNF receptor-associated factor 6

EC=6.3.2.-
Alternative name(s):
E3 ubiquitin-protein ligase TRAF6
Gene names
Name:Traf6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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, 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. Ref.5 Ref.6 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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 TICAM1 and 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. Ref.7 Ref.8 Ref.9 Ref.11 Ref.16 Ref.18 Ref.19 Ref.20

Subcellular location

Cytoplasm By similarity. Cytoplasmcell cortex By similarity. Nucleus By similarity. Lipid droplet. Note: RSAD2/viperin recruits it to the lipid droplet. Ref.20

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.

The MATH/TRAF domain binds to receptor cytoplasmic domains.

Post-translational modification

Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1 By similarity.

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 By similarity.

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. Ref.5 Ref.6 Ref.10 Ref.12 Ref.13 Ref.15 Ref.17

Sequence similarities

Belongs to the TNF receptor-associated factor family. A subfamily.

Contains 1 MATH domain.

Contains 1 RING-type zinc finger.

Contains 2 TRAF-type zinc fingers.

Ontologies

Keywords
   Biological processImmunity
Osteogenesis
Ubl conjugation pathway
   Cellular componentCytoplasm
Lipid droplet
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.17. Source: UniProtKB

JNK cascade

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

T-helper 1 type immune response

Inferred from mutant phenotype Ref.12. Source: MGI

activation of NF-kappaB-inducing kinase activity

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of exogenous peptide antigen via MHC class II

Inferred from mutant phenotype Ref.12. Source: MGI

bone remodeling

Inferred from mutant phenotype Ref.5. Source: UniProtKB

bone resorption

Inferred from mutant phenotype Ref.6. Source: UniProtKB

cell development

Inferred from mutant phenotype Ref.15. Source: MGI

immune response

Inferred from mutant phenotype Ref.15. Source: MGI

interleukin-1-mediated signaling pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

myeloid dendritic cell differentiation

Inferred from mutant phenotype Ref.12. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from mutant phenotype PubMed 11007897. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 14699584. Source: MGI

organ morphogenesis

Inferred from mutant phenotype Ref.15. Source: MGI

ossification

Inferred from mutant phenotype Ref.6. Source: MGI

osteoclast differentiation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.13PubMed 20345905. Source: UniProtKB

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 20345905. Source: UniProtKB

positive regulation of T cell cytokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of interleukin-12 biosynthetic process

Inferred from mutant phenotype Ref.12. Source: MGI

positive regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 biosynthetic process

Inferred from mutant phenotype Ref.12. Source: MGI

positive regulation of lipopolysaccharide-mediated signaling pathway

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

protein K63-linked ubiquitination

Inferred from direct assay PubMed 16252010. Source: UniProtKB

protein autoubiquitination

Traceable author statement PubMed 16378096. Source: UniProtKB

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from direct assay PubMed 23042151. Source: MGI

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

regulation of immunoglobulin secretion

Inferred from direct assay PubMed 12958312. Source: MGI

signal transduction

Inferred from direct assay PubMed 12958312. Source: MGI

   Cellular_componentCD40 receptor complex

Inferred from direct assay PubMed 20614026. Source: BHF-UCL

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20614026. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 16831874. Source: UniProtKB

lipid particle

Inferred from direct assay Ref.20. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionsignal transducer activity

Traceable author statement Ref.6. Source: MGI

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 16252010. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70196-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P70196-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-174: DAGHKCPVDN...CQRPFQKCQV → YLILRKHGAL...TQPPGKLQSP
     175-530: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530TNF receptor-associated factor 6
PRO_0000056408

Regions

Domain358 – 507150MATH
Zinc finger70 – 10940RING-type
Zinc finger150 – 20253TRAF-type 1
Zinc finger203 – 25957TRAF-type 2
Region1 – 362362Interaction with TAX1BP1 By similarity
Coiled coil299 – 35658 Potential

Amino acid modifications

Cross-link124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link461Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence100 – 17475DAGHK…QKCQV → YLILRKHGALQQPNVKSMLE TGHPKNRQTENTGQEHSRMD RNLRQLGSHPSLYYGMNRGL LPCLPTQPPGKLQSP in isoform 2.
VSP_007404
Alternative sequence175 – 530356Missing in isoform 2.
VSP_007405

Experimental info

Sequence conflict2511E → Q in BAA12705. Ref.1
Sequence conflict2511E → Q in BAC30850. Ref.2
Sequence conflict3671N → K in BAA12705. Ref.1
Sequence conflict3671N → K in BAC30850. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: F8389250425E4E2D

FASTA53060,070
        10         20         30         40         50         60 
MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM EEIQGYDVEF 

        70         80         90        100        110        120 
DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD AGHKCPVDNE ILLENQLFPD 

       130        140        150        160        170        180 
NFAKREILSL TVKCPNKGCL QKMELRHLED HQVHCEFALV NCPQCQRPFQ KCQVNTHIIE 

       190        200        210        220        230        240 
DCPRRQVSCV NCAVSMAYEE KEIHDQSCPL ANIICEYCGT ILIREQMPNH YDLDCPTAPI 

       250        260        270        280        290        300 
PCTFSVFGCH EKMQRNHLAR HLQENTQLHM RLLAQAVHNV NLALRPCDAA SPSRGCRPED 

       310        320        330        340        350        360 
PNYEETIKQL ESRLVRQDHQ IRELTAKMET QSMYVGELKR TIRTLEDKVA EMEAQQCNGI 

       370        380        390        400        410        420 
YIWKIGNFGM HLKSQEEERP VVIHSPGFYT GRPGYKLCMR LHLQLPTAQR CANYISLFVH 

       430        440        450        460        470        480 
TMQGEYDSHL PWPFQGTIRL TILDQSEALI RQNHEEVMDA KPELLAFQRP TIPRNPKGFG 

       490        500        510        520        530 
YVTFMHLEAL RQGTFIKDDT LLVRCEVSTR FDMGGLRKEG FQPRSTDAGV 

« Hide

Isoform 2 [UniParc].

Checksum: F66189179AA9F9D3
Show »

FASTA17418,961

References

« Hide 'large scale' references
[1]"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."
Ishida T., Mizushima S., Azuma S., Kobayashi N., Tojo T., Suzuki K., Aizawa S., Watanabe T., Mosialos G., Kieff E., Yamamoto T., Inoue J.
J. Biol. Chem. 271:28745-28748(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/Kaplan.
Tissue: T-cell lymphoma.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Aorta and Vein.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice."
Naito A., Azuma S., Tanaka S., Miyazaki T., Takaki S., Takatsu K., Nakao K., Nakamura K., Katsuki M., Yamamoto T., Inoue J.
Genes Cells 4:353-362(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]"TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling."
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. expand/collapse author list , Lacey D.L., Dunstan C.R., Boyle W.J., Goeddel D.V., Mak T.W.
Genes Dev. 13:1015-1024(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[7]"The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway."
Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.
EMBO J. 19:1576-1586(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND PRKCZ.
[8]"Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin 17 signal transduction."
Schwandner R., Yamaguchi K., Cao Z.
J. Exp. Med. 191:1233-1240(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IL17R.
[9]"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor."
Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J.
J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1; PRKCZ AND NGFR.
[10]"TRAF6-deficient mice display hypohidrotic ectodermal dysplasia."
Naito A., Yoshida H., Nishioka E., Satoh M., Azuma S., Yamamoto T., Nishikawa S., Inoue J.
Proc. Natl. Acad. Sci. U.S.A. 99:8766-8771(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[11]"Tpl2 transduces CD40 and TNF signals that activate ERK and regulates IgE induction by CD40."
Eliopoulos A.G., Wang C.C., Dumitru C.D., Tsichlis P.N.
EMBO J. 22:3855-3864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CD40 AND MAP3K8.
[12]"TRAF6 is a critical factor for dendritic cell maturation and development."
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.
Immunity 19:353-363(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[13]"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."
Gohda J., Matsumura T., Inoue J.
J. Immunol. 173:2913-2917(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[14]"The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination."
Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T., Moscat J.
J. Biol. Chem. 280:35625-35629(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[15]"Dependence of self-tolerance on TRAF6-directed development of thymic stroma."
Akiyama T., Maeda S., Yamane S., Ogino K., Kasai M., Kajiura F., Matsumoto M., Inoue J.
Science 308:248-251(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[16]"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor signaling through direct interaction with the adaptor Pellino-1."
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.
Nat. Immunol. 7:1057-1065(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; MYD88 AND PELI1.
[17]"Characteristics and biological functions of TRAF6."
Inoue J., Gohda J., Akiyama T.
Adv. Exp. Med. Biol. 597:72-79(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[18]"The LIM protein, Limd1, regulates AP-1 activation through an interaction with Traf6 to influence osteoclast development."
Feng Y., Zhao H., Luderer H.F., Epple H., Faccio R., Ross F.P., Teitelbaum S.L., Longmore G.D.
J. Biol. Chem. 282:39-48(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LIMD1.
[19]"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."
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.
J. Biol. Chem. 283:33858-33864(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAFD1.
[20]"Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells."
Saitoh T., Satoh T., Yamamoto N., Uematsu S., Takeuchi O., Kawai T., Akira S.
Immunity 34:352-363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RSAD2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84655 mRNA. Translation: BAA12705.1.
AK041172 mRNA. Translation: BAC30850.1.
AK155434 mRNA. Translation: BAE33263.1.
AL929571 Genomic DNA. Translation: CAM20505.1.
CH466519 Genomic DNA. Translation: EDL27656.1.
CH466519 Genomic DNA. Translation: EDL27657.1.
BC060705 mRNA. Translation: AAH60705.1.
RefSeqNP_033450.2. NM_009424.2.
XP_006499219.1. XM_006499156.1.
UniGeneMm.292729.

3D structure databases

ProteinModelPortalP70196.
SMRP70196. Positions 54-265, 310-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204307. 78 interactions.
DIPDIP-29812N.
IntActP70196. 36 interactions.
MINTMINT-252449.
STRING10090.ENSMUSP00000004949.

PTM databases

PhosphoSiteP70196.

Proteomic databases

PaxDbP70196.
PRIDEP70196.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164. [P70196-1]
GeneID22034.
KEGGmmu:22034.
UCSCuc008lhl.1. mouse. [P70196-2]
uc008lhm.1. mouse. [P70196-1]

Organism-specific databases

CTD7189.
MGIMGI:108072. Traf6.

Phylogenomic databases

eggNOGNOG289765.
GeneTreeENSGT00550000074359.
HOGENOMHOG000006625.
HOVERGENHBG060248.
InParanoidQ6P9M0.
KOK03175.
OMANFQETIH.
OrthoDBEOG7966G5.
PhylomeDBP70196.
TreeFamTF321154.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_98458. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeP70196.
CleanExMM_TRAF6.
GenevestigatorP70196.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027139. TRAF6.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERPTHR10131:SF48. PTHR10131:SF48. 1 hit.
PfamPF00917. MATH. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 3 hits.
PROSITEPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301798.
PROP70196.
SOURCESearch...

Entry information

Entry nameTRAF6_MOUSE
AccessionPrimary (citable) accession number: P70196
Secondary accession number(s): Q6P9M0, Q8BLV2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot