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P70196

- TRAF6_MOUSE

UniProt

P70196 - TRAF6_MOUSE

Protein

TNF receptor-associated factor 6

Gene

Traf6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    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.By similarity7 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri70 – 10940RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri150 – 20253TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri203 – 25957TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. signal transducer activity Source: MGI
    4. ubiquitin conjugating enzyme binding Source: MGI
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of NF-kappaB-inducing kinase activity Source: Ensembl
    2. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: MGI
    3. bone remodeling Source: UniProtKB
    4. bone resorption Source: UniProtKB
    5. cell development Source: MGI
    6. cellular response to lipopolysaccharide Source: MGI
    7. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    8. immune response Source: MGI
    9. interleukin-1-mediated signaling pathway Source: UniProtKB
    10. JNK cascade Source: Ensembl
    11. myeloid dendritic cell differentiation Source: MGI
    12. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    13. neural tube closure Source: UniProtKB
    14. odontogenesis of dentin-containing tooth Source: MGI
    15. organ morphogenesis Source: MGI
    16. ossification Source: MGI
    17. osteoclast differentiation Source: UniProtKB
    18. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    19. positive regulation of interleukin-12 biosynthetic process Source: MGI
    20. positive regulation of interleukin-2 production Source: Ensembl
    21. positive regulation of interleukin-6 biosynthetic process Source: MGI
    22. positive regulation of JUN kinase activity Source: Ensembl
    23. positive regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    24. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    25. positive regulation of osteoclast differentiation Source: Ensembl
    26. positive regulation of smooth muscle cell proliferation Source: Ensembl
    27. positive regulation of T cell cytokine production Source: Ensembl
    28. positive regulation of T cell proliferation Source: UniProtKB
    29. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    30. positive regulation of transcription regulatory region DNA binding Source: Ensembl
    31. protein autoubiquitination Source: UniProtKB
    32. protein complex assembly Source: Ensembl
    33. protein K63-linked ubiquitination Source: UniProtKB
    34. protein ubiquitination Source: MGI
    35. regulation of apoptotic process Source: InterPro
    36. regulation of immunoglobulin secretion Source: MGI
    37. signal transduction Source: MGI
    38. T cell receptor signaling pathway Source: Ensembl
    39. T-helper 1 type immune response Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Immunity, Osteogenesis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_198536. IRAK2 mediated activation of TAK1 complex.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_198690. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_202271. NRIF signals cell death from the nucleus.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 6 (EC:6.3.2.-)
    Alternative name(s):
    E3 ubiquitin-protein ligase TRAF6
    Gene namesi
    Name:Traf6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:108072. Traf6.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcell cortex By similarity. Nucleus By similarity. Lipid droplet 1 Publication
    Note: RSAD2/viperin recruits it to the lipid droplet.

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cell cortex Source: UniProtKB-SubCell
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. cytosol Source: UniProtKB
    5. lipid particle Source: UniProtKB
    6. nuclear membrane Source: Ensembl
    7. perinuclear region of cytoplasm Source: Ensembl
    8. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Lipid droplet, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    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.7 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530TNF receptor-associated factor 6PRO_0000056408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki461 – 461Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP70196.
    PRIDEiP70196.

    PTM databases

    PhosphoSiteiP70196.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, lung, liver, skeletal muscle, and kidney; lower expression in heart, spleen, and testis.

    Gene expression databases

    BgeeiP70196.
    CleanExiMM_TRAF6.
    GenevestigatoriP70196.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cd40P275122EBI-448028,EBI-525742
    EcsitQ9QZH64EBI-448028,EBI-527020
    Hspa1bP178793EBI-448028,EBI-397360
    Irak1Q62406-14EBI-448028,EBI-488313
    Irak3Q8K4B23EBI-448028,EBI-646179
    Map3k3Q610845EBI-448028,EBI-446250
    Nr0b2Q622275EBI-448028,EBI-4310440
    Ptpn11P352352EBI-448028,EBI-397236
    TifaQ793I82EBI-448028,EBI-524817
    Tnfrsf11aO353052EBI-448028,EBI-647362
    Traf3ip2Q8C0E53EBI-448028,EBI-530713
    Traf3ip2Q8N7N64EBI-448028,EBI-646165
    Trafd1Q3UDK12EBI-448028,EBI-1396948
    UbcP629912EBI-448028,EBI-413074

    Protein-protein interaction databases

    BioGridi204307. 80 interactions.
    DIPiDIP-29812N.
    IntActiP70196. 36 interactions.
    MINTiMINT-252449.
    STRINGi10090.ENSMUSP00000004949.

    Structurei

    3D structure databases

    ProteinModelPortaliP70196.
    SMRiP70196. Positions 54-210, 317-516.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini358 – 507150MATHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 362362Interaction with TAX1BP1By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili299 – 35658Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domain mediates homo- and hetero-oligomerization.
    The MATH/TRAF domain binds to receptor cytoplasmic domains.

    Sequence similaritiesi

    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri70 – 10940RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri150 – 20253TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri203 – 25957TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG289765.
    GeneTreeiENSGT00550000074359.
    HOGENOMiHOG000006625.
    HOVERGENiHBG060248.
    InParanoidiQ6P9M0.
    KOiK03175.
    OMAiNFQETIH.
    OrthoDBiEOG7966G5.
    PhylomeDBiP70196.
    TreeFamiTF321154.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR002083. 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]
    PANTHERiPTHR10131:SF52. PTHR10131:SF52. 1 hit.
    PfamiPF00917. MATH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015614. TRAF. 1 hit.
    SMARTiSM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 3 hits.
    PROSITEiPS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70196-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM    50
    EEIQGYDVEF DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD 100
    AGHKCPVDNE ILLENQLFPD NFAKREILSL TVKCPNKGCL QKMELRHLED 150
    HQVHCEFALV NCPQCQRPFQ KCQVNTHIIE DCPRRQVSCV NCAVSMAYEE 200
    KEIHDQSCPL ANIICEYCGT ILIREQMPNH YDLDCPTAPI PCTFSVFGCH 250
    EKMQRNHLAR HLQENTQLHM RLLAQAVHNV NLALRPCDAA SPSRGCRPED 300
    PNYEETIKQL ESRLVRQDHQ IRELTAKMET QSMYVGELKR TIRTLEDKVA 350
    EMEAQQCNGI YIWKIGNFGM HLKSQEEERP VVIHSPGFYT GRPGYKLCMR 400
    LHLQLPTAQR CANYISLFVH TMQGEYDSHL PWPFQGTIRL TILDQSEALI 450
    RQNHEEVMDA KPELLAFQRP TIPRNPKGFG YVTFMHLEAL RQGTFIKDDT 500
    LLVRCEVSTR FDMGGLRKEG FQPRSTDAGV 530
    Length:530
    Mass (Da):60,070
    Last modified:February 9, 2010 - v2
    Checksum:iF8389250425E4E2D
    GO
    Isoform 2 (identifier: P70196-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:174
    Mass (Da):18,961
    Checksum:iF66189179AA9F9D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511E → Q in BAA12705. (PubMed:8910514)Curated
    Sequence conflicti251 – 2511E → Q in BAC30850. (PubMed:16141072)Curated
    Sequence conflicti367 – 3671N → K in BAA12705. (PubMed:8910514)Curated
    Sequence conflicti367 – 3671N → K in BAC30850. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei100 – 17475DAGHK…QKCQV → YLILRKHGALQQPNVKSMLE TGHPKNRQTENTGQEHSRMD RNLRQLGSHPSLYYGMNRGL LPCLPTQPPGKLQSP in isoform 2. 1 PublicationVSP_007404Add
    BLAST
    Alternative sequencei175 – 530356Missing in isoform 2. 1 PublicationVSP_007405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS16464.1. [P70196-1]
    RefSeqiNP_033450.2. NM_009424.2. [P70196-1]
    XP_006499219.1. XM_006499156.1. [P70196-1]
    UniGeneiMm.292729.

    Genome annotation databases

    EnsembliENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164. [P70196-1]
    GeneIDi22034.
    KEGGimmu:22034.
    UCSCiuc008lhl.1. mouse. [P70196-2]
    uc008lhm.1. mouse. [P70196-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS16464.1. [P70196-1 ]
    RefSeqi NP_033450.2. NM_009424.2. [P70196-1 ]
    XP_006499219.1. XM_006499156.1. [P70196-1 ]
    UniGenei Mm.292729.

    3D structure databases

    ProteinModelPortali P70196.
    SMRi P70196. Positions 54-210, 317-516.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204307. 80 interactions.
    DIPi DIP-29812N.
    IntActi P70196. 36 interactions.
    MINTi MINT-252449.
    STRINGi 10090.ENSMUSP00000004949.

    PTM databases

    PhosphoSitei P70196.

    Proteomic databases

    PaxDbi P70196.
    PRIDEi P70196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004949 ; ENSMUSP00000004949 ; ENSMUSG00000027164 . [P70196-1 ]
    GeneIDi 22034.
    KEGGi mmu:22034.
    UCSCi uc008lhl.1. mouse. [P70196-2 ]
    uc008lhm.1. mouse. [P70196-1 ]

    Organism-specific databases

    CTDi 7189.
    MGIi MGI:108072. Traf6.

    Phylogenomic databases

    eggNOGi NOG289765.
    GeneTreei ENSGT00550000074359.
    HOGENOMi HOG000006625.
    HOVERGENi HBG060248.
    InParanoidi Q6P9M0.
    KOi K03175.
    OMAi NFQETIH.
    OrthoDBi EOG7966G5.
    PhylomeDBi P70196.
    TreeFami TF321154.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_198536. IRAK2 mediated activation of TAK1 complex.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_198543. IRAK1 recruits IKK complex.
    REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_198690. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_202271. NRIF signals cell death from the nucleus.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_224208. Interleukin-1 signaling.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    NextBioi 301798.
    PROi P70196.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70196.
    CleanExi MM_TRAF6.
    Genevestigatori P70196.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR002083. 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 ]
    PANTHERi PTHR10131:SF52. PTHR10131:SF52. 1 hit.
    Pfami PF00917. MATH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015614. TRAF. 1 hit.
    SMARTi SM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 3 hits.
    PROSITEi PS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiTRAF6_MOUSE
    AccessioniPrimary (citable) accession number: P70196
    Secondary accession number(s): Q6P9M0, Q8BLV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3