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Q9Y4K3

- TRAF6_HUMAN

UniProt

Q9Y4K3 - TRAF6_HUMAN

Protein

TNF receptor-associated factor 6

Gene

TRAF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. 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.11 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. histone deacetylase binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase B binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. protein N-terminus binding Source: UniProtKB
    8. signal transducer activity Source: InterPro
    9. thioesterase binding Source: UniProtKB
    10. tumor necrosis factor receptor binding Source: UniProt
    11. ubiquitin conjugating enzyme binding Source: MGI
    12. ubiquitin protein ligase binding Source: UniProtKB
    13. ubiquitin-protein transferase activity Source: UniProtKB
    14. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
    3. activation of protein kinase activity Source: UniProtKB
    4. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Ensembl
    5. apoptotic signaling pathway Source: Reactome
    6. bone resorption Source: Ensembl
    7. cell development Source: Ensembl
    8. cellular response to lipopolysaccharide Source: MGI
    9. Fc-epsilon receptor signaling pathway Source: Reactome
    10. I-kappaB kinase/NF-kappaB signaling Source: Reactome
    11. innate immune response Source: Reactome
    12. interleukin-1-mediated signaling pathway Source: Ensembl
    13. JNK cascade Source: Reactome
    14. membrane protein intracellular domain proteolysis Source: Reactome
    15. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    16. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    17. myeloid dendritic cell differentiation Source: Ensembl
    18. negative regulation of apoptotic process Source: Reactome
    19. negative regulation of transcription, DNA-templated Source: UniProtKB
    20. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    21. neural tube closure Source: Ensembl
    22. neurotrophin TRK receptor signaling pathway Source: Reactome
    23. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    24. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    25. odontogenesis of dentin-containing tooth Source: Ensembl
    26. ossification Source: UniProtKB-KW
    27. osteoclast differentiation Source: Ensembl
    28. positive regulation of apoptotic process Source: Reactome
    29. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    30. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
    31. positive regulation of interleukin-2 production Source: UniProtKB
    32. positive regulation of interleukin-6 biosynthetic process Source: Ensembl
    33. positive regulation of JUN kinase activity Source: UniProtKB
    34. positive regulation of lipopolysaccharide-mediated signaling pathway Source: Ensembl
    35. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    36. positive regulation of osteoclast differentiation Source: UniProtKB
    37. positive regulation of protein ubiquitination Source: BHF-UCL
    38. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    39. positive regulation of smooth muscle cell proliferation Source: Ensembl
    40. positive regulation of T cell activation Source: UniProtKB
    41. positive regulation of T cell cytokine production Source: UniProtKB
    42. positive regulation of T cell proliferation Source: Ensembl
    43. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    44. positive regulation of transcription regulatory region DNA binding Source: BHF-UCL
    45. protein autoubiquitination Source: UniProtKB
    46. protein complex assembly Source: Ensembl
    47. protein K63-linked ubiquitination Source: UniProtKB
    48. protein polyubiquitination Source: UniProtKB
    49. regulation of immunoglobulin secretion Source: Ensembl
    50. response to interleukin-1 Source: UniProtKB
    51. stress-activated MAPK cascade Source: Reactome
    52. T cell receptor signaling pathway Source: UniProtKB
    53. T-helper 1 type immune response Source: Ensembl
    54. toll-like receptor 10 signaling pathway Source: Reactome
    55. toll-like receptor 2 signaling pathway Source: Reactome
    56. toll-like receptor 3 signaling pathway Source: Reactome
    57. toll-like receptor 4 signaling pathway Source: Reactome
    58. toll-like receptor 5 signaling pathway Source: Reactome
    59. toll-like receptor 9 signaling pathway Source: Reactome
    60. toll-like receptor signaling pathway Source: Reactome
    61. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    62. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    63. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Immunity, Osteogenesis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ9Y4K3.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 6 (EC:6.3.2.-)
    Alternative name(s):
    E3 ubiquitin-protein ligase TRAF6
    Interleukin-1 signal transducer
    RING finger protein 85
    Gene namesi
    Name:TRAF6
    Synonyms:RNF85
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:12036. TRAF6.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcell cortex 1 Publication. Nucleus 1 Publication. Lipid droplet By similarity
    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.By similarity

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cell cortex Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytoplasmic side of plasma membrane Source: BHF-UCL
    5. cytosol Source: Reactome
    6. endosome membrane Source: Reactome
    7. lipid particle Source: UniProtKB
    8. mitochondrion Source: HPA
    9. nucleolus Source: HPA
    10. nucleus Source: UniProtKB
    11. perinuclear region of cytoplasm Source: BHF-UCL
    12. plasma membrane Source: UniProtKB
    13. protein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Lipid droplet, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571D → K: Loss of interaction with UBE2N. 1 Publication
    Mutagenesisi70 – 701C → A: Loss of ligase activity, autoubiquitination and signaling capacity. 2 Publications
    Mutagenesisi72 – 721I → D: Loss of interaction with UBE2N. 1 Publication
    Mutagenesisi74 – 741L → E or K: Loss of interaction with UBE2N. 1 Publication
    Mutagenesisi88 – 881R → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-122. 1 Publication
    Mutagenesisi118 – 1181F → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. 1 Publication
    Mutagenesisi118 – 1181F → W: Partially impaired polyubiquitin synthesis. 1 Publication
    Mutagenesisi118 – 1181F → Y: Partially impaired polyubiquitin synthesis. 1 Publication
    Mutagenesisi122 – 1221F → A: Loss of TRAF6 homodimerization and partially impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-88. 1 Publication
    Mutagenesisi124 – 1241K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 3 Publications
    Mutagenesisi142 – 1421K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication
    Mutagenesisi453 – 4531K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication

    Organism-specific databases

    Orphaneti1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
    PharmGKBiPA36713.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522TNF receptor-associated factor 6PRO_0000056407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1.1 Publication
    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.6 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y4K3.
    PaxDbiQ9Y4K3.
    PRIDEiQ9Y4K3.

    PTM databases

    PhosphoSiteiQ9Y4K3.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    BgeeiQ9Y4K3.
    CleanExiHS_TRAF6.
    GenevestigatoriQ9Y4K3.

    Organism-specific databases

    HPAiCAB004605.
    HPA019805.
    HPA020599.

    Interactioni

    Subunit structurei

    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 TICAM1 and TICAM2. Interacts with CARD14. Interacts with CD40 and MAP3K8; the interaction is required for ERK activation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q8V2D13EBI-359276,EBI-8622036From a different organism.
    CD40P259422EBI-359276,EBI-525714
    EcsitQ9QZH62EBI-359276,EBI-527020From a different organism.
    IL1R1P147782EBI-359276,EBI-525905
    IRAK1P516172EBI-359276,EBI-358664
    MALT1Q9UDY83EBI-359276,EBI-1047372
    MAP3K14Q995582EBI-359276,EBI-358011
    MAP3K7O433182EBI-359276,EBI-358684
    NgfrP071742EBI-359276,EBI-1038810From a different organism.
    RUSC1Q9BVN2-22EBI-359276,EBI-6257338
    SPHK1Q9NYA12EBI-359276,EBI-985303
    SQSTM1Q135012EBI-359276,EBI-307104
    TAX1BP1Q86VP18EBI-359276,EBI-529518
    TRAF1Q130773EBI-359276,EBI-359224
    TRAF2Q129333EBI-359276,EBI-355744
    TRAF5O004633EBI-359276,EBI-523498
    UBCP0CG483EBI-359276,EBI-3390054
    UBE2D1P516682EBI-359276,EBI-743540
    UBE2D2P628372EBI-359276,EBI-347677
    UBE2D3P610772EBI-359276,EBI-348268
    UBE2NP610883EBI-359276,EBI-1052908
    VACWR178Q012202EBI-359276,EBI-3863691From a different organism.
    XIAPP981702EBI-359276,EBI-517127
    ZNF675Q8TD234EBI-359276,EBI-528190

    Protein-protein interaction databases

    BioGridi113041. 221 interactions.
    DIPiDIP-27515N.
    IntActiQ9Y4K3. 84 interactions.
    MINTiMINT-88585.
    STRINGi9606.ENSP00000316840.

    Structurei

    Secondary structure

    1
    522
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 623
    Helixi66 – 683
    Turni71 – 733
    Beta strandi78 – 825
    Turni84 – 863
    Beta strandi88 – 903
    Helixi91 – 10111
    Turni106 – 1083
    Helixi114 – 1163
    Helixi121 – 1288
    Beta strandi130 – 1334
    Beta strandi135 – 1384
    Beta strandi142 – 1443
    Helixi145 – 1473
    Helixi149 – 1513
    Beta strandi153 – 1553
    Beta strandi158 – 1614
    Turni163 – 1653
    Beta strandi168 – 1703
    Helixi171 – 1733
    Helixi174 – 1807
    Beta strandi186 – 1883
    Turni190 – 1923
    Beta strandi195 – 1973
    Helixi198 – 2003
    Helixi201 – 2055
    Beta strandi351 – 3577
    Helixi360 – 3689
    Beta strandi373 – 3764
    Beta strandi380 – 3856
    Beta strandi388 – 3958
    Turni401 – 4055
    Beta strandi406 – 4149
    Helixi419 – 4213
    Beta strandi428 – 4347
    Helixi440 – 4423
    Beta strandi446 – 4516
    Helixi457 – 4593
    Beta strandi463 – 4664
    Beta strandi468 – 47811
    Helixi479 – 4835
    Turni484 – 4863
    Beta strandi492 – 5009

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LB4X-ray2.40A348-504[»]
    1LB5X-ray2.40A347-504[»]
    1LB6X-ray1.80A347-504[»]
    2ECINMR-A50-128[»]
    2JMDNMR-A67-124[»]
    3HCSX-ray2.20A/B50-211[»]
    3HCTX-ray2.10A50-159[»]
    3HCUX-ray2.60A/C50-159[»]
    ProteinModelPortaliQ9Y4K3.
    SMRiQ9Y4K3. Positions 54-210, 302-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y4K3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini350 – 499150MATHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 354354Interaction with TAX1BP1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili288 – 34861Sequence 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.
    HOGENOMiHOG000006625.
    HOVERGENiHBG060248.
    InParanoidiQ9Y4K3.
    KOiK03175.
    OMAiNFQETIH.
    OrthoDBiEOG7966G5.
    PhylomeDBiQ9Y4K3.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9Y4K3-1 [UniParc]FASTAAdd to Basket

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    MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM    50
    EEIQGYDVEF DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD 100
    AGHKCPVDNE ILLENQLFPD NFAKREILSL MVKCPNEGCL HKMELRHLED 150
    HQAHCEFALM DCPQCQRPFQ KFHINIHILK DCPRRQVSCD NCAASMAFED 200
    KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI PCTFSTFGCH 250
    EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH 300
    QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN 350
    GIYIWKIGNF GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA 400
    QRCANYISLF VHTMQGEYDS HLPWPFQGTI RLTILDQSEA PVRQNHEEIM 450
    DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE ALRQRTFIKD DTLLVRCEVS 500
    TRFDMGSLRR EGFQPRSTDA GV 522
    Length:522
    Mass (Da):59,573
    Last modified:November 1, 1999 - v1
    Checksum:i5AB9C255CCFEE749
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121S → F in AAH31052. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78798 mRNA. Translation: AAB38751.1.
    AY228337 Genomic DNA. Translation: AAO38054.1.
    AK292978 mRNA. Translation: BAF85667.1.
    AC009656 Genomic DNA. No translation available.
    AC061999 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68119.1.
    CH471064 Genomic DNA. Translation: EAW68120.1.
    CH471064 Genomic DNA. Translation: EAW68122.1.
    BC031052 mRNA. Translation: AAH31052.1.
    CCDSiCCDS7901.1.
    PIRiS71821.
    RefSeqiNP_004611.1. NM_004620.3.
    NP_665802.1. NM_145803.2.
    UniGeneiHs.444172.
    Hs.591983.

    Genome annotation databases

    EnsembliENST00000348124; ENSP00000337853; ENSG00000175104.
    ENST00000526995; ENSP00000433623; ENSG00000175104.
    GeneIDi7189.
    KEGGihsa:7189.
    UCSCiuc001mwq.2. human.

    Polymorphism databases

    DMDMi30580642.

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78798 mRNA. Translation: AAB38751.1 .
    AY228337 Genomic DNA. Translation: AAO38054.1 .
    AK292978 mRNA. Translation: BAF85667.1 .
    AC009656 Genomic DNA. No translation available.
    AC061999 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68119.1 .
    CH471064 Genomic DNA. Translation: EAW68120.1 .
    CH471064 Genomic DNA. Translation: EAW68122.1 .
    BC031052 mRNA. Translation: AAH31052.1 .
    CCDSi CCDS7901.1.
    PIRi S71821.
    RefSeqi NP_004611.1. NM_004620.3.
    NP_665802.1. NM_145803.2.
    UniGenei Hs.444172.
    Hs.591983.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LB4 X-ray 2.40 A 348-504 [» ]
    1LB5 X-ray 2.40 A 347-504 [» ]
    1LB6 X-ray 1.80 A 347-504 [» ]
    2ECI NMR - A 50-128 [» ]
    2JMD NMR - A 67-124 [» ]
    3HCS X-ray 2.20 A/B 50-211 [» ]
    3HCT X-ray 2.10 A 50-159 [» ]
    3HCU X-ray 2.60 A/C 50-159 [» ]
    ProteinModelPortali Q9Y4K3.
    SMRi Q9Y4K3. Positions 54-210, 302-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113041. 221 interactions.
    DIPi DIP-27515N.
    IntActi Q9Y4K3. 84 interactions.
    MINTi MINT-88585.
    STRINGi 9606.ENSP00000316840.

    PTM databases

    PhosphoSitei Q9Y4K3.

    Polymorphism databases

    DMDMi 30580642.

    Proteomic databases

    MaxQBi Q9Y4K3.
    PaxDbi Q9Y4K3.
    PRIDEi Q9Y4K3.

    Protocols and materials databases

    DNASUi 7189.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348124 ; ENSP00000337853 ; ENSG00000175104 .
    ENST00000526995 ; ENSP00000433623 ; ENSG00000175104 .
    GeneIDi 7189.
    KEGGi hsa:7189.
    UCSCi uc001mwq.2. human.

    Organism-specific databases

    CTDi 7189.
    GeneCardsi GC11M036467.
    HGNCi HGNC:12036. TRAF6.
    HPAi CAB004605.
    HPA019805.
    HPA020599.
    MIMi 602355. gene.
    neXtProti NX_Q9Y4K3.
    Orphaneti 1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
    PharmGKBi PA36713.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289765.
    HOGENOMi HOG000006625.
    HOVERGENi HBG060248.
    InParanoidi Q9Y4K3.
    KOi K03175.
    OMAi NFQETIH.
    OrthoDBi EOG7966G5.
    PhylomeDBi Q9Y4K3.
    TreeFami TF321154.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25024. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25222. MyD88 dependent cascade initiated on endosome.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_6788. MyD88:Mal cascade initiated on plasma membrane.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q9Y4K3.

    Miscellaneous databases

    ChiTaRSi Traf6. human.
    EvolutionaryTracei Q9Y4K3.
    GeneWikii TRAF6.
    GenomeRNAii 7189.
    NextBioi 28192.
    PROi Q9Y4K3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y4K3.
    CleanExi HS_TRAF6.
    Genevestigatori Q9Y4K3.

    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. "TRAF6 is a signal transducer for interleukin-1."
      Cao Z., Xiong J., Takeuchi M., Kurama T., Goeddel D.V.
      Nature 383:443-446(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IRAK1.
    2. SeattleSNPs variation discovery resource
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Trachea.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Testis.
    7. "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1."
      Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.
      Nature 385:540-544(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K14.
    8. "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling."
      Muzio M., Ni J., Feng P., Dixit V.M.
      Science 278:1612-1615(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK2.
    9. "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."
      McCarthy J.V., Ni J., Dixit V.M.
      J. Biol. Chem. 273:16968-16975(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIPK2.
    10. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
      Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
      J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF11A.
    11. "Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway."
      Kashiwada M., Shirakata Y., Inoue J., Nakano H., Okazaki K., Okumura K., Yamamoto T., Nagaoka H., Takemori T.
      J. Exp. Med. 187:237-244(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF5.
    12. Cited for: INTERACTION WITH MAP3K5.
    13. "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."
      Baud V., Liu Z.-G., Bennett B., Suzuki N., Xia Y., Karin M.
      Genes Dev. 13:1297-1308(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K1.
    14. "Association of the p75 neurotrophin receptor with TRAF6."
      Khursigara G., Orlinick J.R., Chao M.V.
      J. Biol. Chem. 274:2597-2600(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGFR.
    15. "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family."
      Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.
      J. Biol. Chem. 274:19403-19410(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK3.
    16. "TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction."
      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.
      J. Biol. Chem. 274:30202-30208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGFR.
    17. "TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src."
      Wong B.R., Besser D., Kim N., Arron J.R., Vologodskaia M., Hanafusa H., Choi Y.
      Mol. Cell 4:1041-1049(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF11A AND CSK.
    18. "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway."
      Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.
      Nature 398:252-256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K7 AND TAB1.
    19. "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)."
      Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.
      Oncogene 18:5814-5820(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K5.
    20. "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain."
      Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J.
      Cell 103:351-361(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2V1, FUNCTION AS AN E3 UBIQUITIN LIGASE.
    21. "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."
      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.
      J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TDP2.
    22. "B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1."
      Shu H.-B., Johnson H.
      Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF17.
    23. "T6BP, a TRAF6-interacting protein involved in IL-1 signaling."
      Ling L., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 97:9567-9572(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAX1BP1.
    24. "TAK1 is a ubiquitin-dependent kinase of MKK and IKK."
      Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.
      Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    25. "NF-kappaB activator Act1 associates with IL-1/Toll pathway adaptor molecule TRAF6."
      Kanamori M., Kai C., Hayashizaki Y., Suzuki H.
      FEBS Lett. 532:241-246(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF3IP2.
    26. "A novel zinc finger protein that inhibits osteoclastogenesis and the function of tumor necrosis factor receptor-associated factor 6."
      Shin J.N., Kim I., Lee J.S., Koh G.Y., Lee Z.H., Kim H.-H.
      J. Biol. Chem. 277:8346-8353(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF675.
    27. "IRAK4: a novel member of the IRAK family with the properties of an IRAK-kinase."
      Li S., Strelow A., Fontana E.J., Wesche H.
      Proc. Natl. Acad. Sci. U.S.A. 99:5567-5572(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK4.
    28. "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."
      Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X.
      J. Biol. Chem. 278:10952-10956(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELI1.
    29. "Pellino2 activates the mitogen activated protein kinase pathway."
      Jensen L.E., Whitehead A.S.
      FEBS Lett. 545:199-202(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELI1 AND PELI2.
    30. "TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing adapter protein involved in TIR signaling."
      Bin L.-H., Xu L.-G., Shu H.-B.
      J. Biol. Chem. 278:24526-24532(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM2.
    31. "Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein."
      Jensen L.E., Whitehead A.S.
      J. Immunol. 171:1500-1506(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELI3.
    32. "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."
      Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K., Akira S.
      J. Immunol. 171:4304-4310(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    33. "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
      Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
      J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    34. "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation."
      Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z., Shu H.-B.
      J. Biol. Chem. 279:16847-16853(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFAND5.
    35. Cited for: INTERACTION WITH EIF2AK2.
    36. "Toll-like receptor 3-mediated activation of NF-kappaB and IRF3 diverges at Toll-IL-1 receptor domain-containing adapter inducing IFN-beta."
      Jiang Z., Mak T.W., Sen G., Li X.
      Proc. Natl. Acad. Sci. U.S.A. 101:3533-3538(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    37. "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."
      Seth R.B., Sun L., Ea C.-K., Chen Z.J.
      Cell 122:669-682(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAVS.
    38. "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."
      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.
      Immunity 23:479-490(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL1RL1.
    39. "FLN29, a novel interferon- and LPS-inducible gene acting as a negative regulator of toll-like receptor signaling."
      Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T., Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.
      J. Biol. Chem. 280:41289-41297(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAFD1.
    40. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
      Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
      Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAVS.
    41. "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."
      Feng Y., Longmore G.D.
      Mol. Cell. Biol. 25:4010-4022(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AJUBA.
    42. "Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling."
      Wang Y., Tang Y., Teng L., Wu Y., Zhao X., Pei G.
      Nat. Immunol. 7:139-147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION OF NF-KAPPA-B AND JUN, INTERACTION WITH ARBB1 AND ARBB2.
    43. "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.
    44. "Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation."
      Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.
      J. Biol. Chem. 282:4102-4112(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-70 AND LYS-124, UBIQUITINATION AT LYS-124, FUNCTION.
    45. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
      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.
      J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBCK1.
    46. "Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
      Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
      J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, SUMOYLATION AT LYS-124; LYS-142 AND LYS-453, UBIQUITINATION, INTERACTION WITH HDAC1 AND RANGAP1, MUTAGENESIS OF LYS-124; LYS-142 AND LYS-453.
    47. "Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation."
      Conze D.B., Wu C.J., Thomas J.A., Landstrom A., Ashwell J.D.
      Mol. Cell. Biol. 28:3538-3547(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OR IRAK1.
    48. "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner."
      Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V., Schuster N., Zhang S., Heldin C.H., Landstrom M.
      Nat. Cell Biol. 10:1199-1207(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TGFBR1, UBIQUITINATION.
    49. "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."
      Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.
      Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WDR34.
    50. "Direct activation of protein kinases by unanchored polyubiquitin chains."
      Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J.
      Nature 461:114-119(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION.
    51. Cited for: FUNCTION.
    52. "NUMBL interacts with TRAF6 and promotes the degradation of TRAF6."
      Zhou L., Ma Q., Shi H., Huo K.
      Biochem. Biophys. Res. Commun. 392:409-414(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUMBL.
    53. "Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kappaB activation and endoplasmic reticulum stress-induced cell death."
      Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.
      J. Cell. Physiol. 226:3121-3131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARD14.
    54. "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1."
      Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.
      J. Immunol. 187:2559-2568(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT3.
    55. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-506 OF APOPROTEIN AND IN COMPLEXES WITH TNFRSF5 AND TNFRSF11A PEPTIDES, FUNCTION, SUBUNIT.
    56. "Structure, interactions, and dynamics of the RING domain from human TRAF6."
      Mercier P., Lewis M.J., Hau D.D., Saltibus L.F., Xiao W., Spyracopoulos L.
      Protein Sci. 16:602-614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 63-124 IN COMPLEX WITH ZINC IONS, INTERACTION WITH UBE2N.
    57. "Solution structure of the RING domain of the human TNF receptor-associated factor 6 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 43-128.
    58. Cited for: 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, ZINC-FINGER.

    Entry informationi

    Entry nameiTRAF6_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4K3
    Secondary accession number(s): A6NKI7
    , A8KAB3, D3DR16, Q8NEH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3