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Q9Y4K3 (TRAF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
Interleukin-1 signal transducer
RING finger protein 85
Gene names
Name:TRAF6
Synonyms:RNF85
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 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. 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.1 Ref.20 Ref.42 Ref.44 Ref.46 Ref.47 Ref.49 Ref.50 Ref.54 Ref.57

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.57

Subcellular location

Cytoplasm. Cytoplasmcell cortex. Nucleus. 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. Ref.46

Tissue specificity

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

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-453 with SUMO1. Ref.46

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.

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
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

T-helper 1 type immune response

Inferred from electronic annotation. Source: Ensembl

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

activation of NF-kappaB-inducing kinase activity

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

activation of protein kinase activity

Inferred from direct assay Ref.44. Source: UniProtKB

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

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Traceable author statement. Source: Reactome

bone resorption

Inferred from electronic annotation. Source: Ensembl

cell development

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 23776175. Source: MGI

innate immune response

Traceable author statement. Source: Reactome

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

membrane protein intracellular domain proteolysis

Traceable author statement. Source: Reactome

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.46. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.46. Source: UniProtKB

neural tube closure

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from direct assay Ref.44. Source: UniProtKB

positive regulation of JUN kinase activity

Non-traceable author statement Ref.44. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 11279055Ref.42. Source: UniProtKB

positive regulation of T cell activation

Inferred by curator PubMed 15125833. Source: UniProtKB

positive regulation of T cell cytokine production

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of interleukin-12 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-2 production

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

positive regulation of interleukin-6 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from direct assay Ref.44. Source: UniProtKB

positive regulation of protein ubiquitination

Non-traceable author statement PubMed 22412986. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 12296995. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.26. Source: BHF-UCL

positive regulation of transcription regulatory region DNA binding

Inferred from direct assay Ref.26. Source: BHF-UCL

protein K63-linked ubiquitination

Inferred from direct assay Ref.50. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.44Ref.46. Source: UniProtKB

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from direct assay PubMed 15125833Ref.49. Source: UniProtKB

regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from direct assay Ref.44. Source: UniProtKB

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.42Ref.46. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

lipid particle

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.46. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.26. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.46. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 23776175. Source: MGI

   Molecular_functionhistone deacetylase binding

Inferred from physical interaction Ref.46. Source: UniProtKB

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.32. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18PubMed 11244088PubMed 11279055PubMed 11397809Ref.26Ref.25Ref.36Ref.35PubMed 15125833Ref.42Ref.45Ref.46Ref.47Ref.51Ref.53. Source: UniProtKB

protein kinase B binding

Inferred from physical interaction Ref.50. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.50. Source: UniProtKB

thioesterase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin conjugating enzyme binding

Inferred from direct assay PubMed 23776175. Source: MGI

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 15125833Ref.44Ref.50. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522TNF receptor-associated factor 6
PRO_0000056407

Regions

Domain350 – 499150MATH
Zinc finger70 – 10940RING-type
Zinc finger150 – 20253TRAF-type 1
Zinc finger203 – 25957TRAF-type 2
Region1 – 354354Interaction with TAX1BP1
Coiled coil288 – 34861 Potential

Amino acid modifications

Cross-link124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.44 Ref.46
Cross-link124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-link142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.46
Cross-link453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.46

Experimental info

Mutagenesis571D → K: Loss of interaction with UBE2N. Ref.57
Mutagenesis701C → A: Loss of ligase activity, autoubiquitination and signaling capacity. Ref.44 Ref.57
Mutagenesis721I → D: Loss of interaction with UBE2N. Ref.57
Mutagenesis741L → E or K: Loss of interaction with UBE2N. Ref.57
Mutagenesis881R → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-122. Ref.57
Mutagenesis1181F → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Ref.57
Mutagenesis1181F → W: Partially impaired polyubiquitin synthesis. Ref.57
Mutagenesis1181F → Y: Partially impaired polyubiquitin synthesis. Ref.57
Mutagenesis1221F → A: Loss of TRAF6 homodimerization and partially impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-88. Ref.57
Mutagenesis1241K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. Ref.44 Ref.46 Ref.57
Mutagenesis1421K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. Ref.46
Mutagenesis4531K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. Ref.46
Sequence conflict121S → F in AAH31052. Ref.6

Secondary structure

.............................................................................. 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y4K3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 5AB9C255CCFEE749

FASTA52259,573
        10         20         30         40         50         60 
MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM EEIQGYDVEF 

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

       130        140        150        160        170        180 
NFAKREILSL MVKCPNEGCL HKMELRHLED HQAHCEFALM DCPQCQRPFQ KFHINIHILK 

       190        200        210        220        230        240 
DCPRRQVSCD NCAASMAFED KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI 

       250        260        270        280        290        300 
PCTFSTFGCH EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH 

       310        320        330        340        350        360 
QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN GIYIWKIGNF 

       370        380        390        400        410        420 
GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA QRCANYISLF VHTMQGEYDS 

       430        440        450        460        470        480 
HLPWPFQGTI RLTILDQSEA PVRQNHEEIM DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE 

       490        500        510        520 
ALRQRTFIKD DTLLVRCEVS TRFDMGSLRR EGFQPRSTDA GV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ASK1 is essential for JNK/SAPK activation by TRAF2."
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M., Miyazono K., Ichijo H.
Mol. Cell 2:389-395(1998) [PubMed] [Europe PMC] [Abstract]
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]"TRAF family proteins link PKR with NF-kappa B activation."
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H., Alcami J., Esteban M.
Mol. Cell. Biol. 24:4502-4512(2004) [PubMed] [Europe PMC] [Abstract]
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]"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.
[48]"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.
[49]"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.
[50]"The E3 ligase TRAF6 regulates Akt ubiquitination and activation."
Yang W.-L., Wang J., Chan C.-H., Lee S.-W., Campos A.D., Lamothe B., Hur L., Grabiner B.C., Lin X., Darnay B.G., Lin H.-K.
Science 325:1134-1138(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[51]"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.
[52]"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.
[53]"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.
[54]"Distinct molecular mechanism for initiating TRAF6 signalling."
Ye H., Arron J.R., Lamothe B., Cirilli M., Kobayashi T., Shevde N.K., Segal D., Dzivenu O.K., Vologodskaia M., Yim M., Du K., Singh S., Pike J.W., Darnay B.G., Choi Y., Wu H.
Nature 418:443-447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-506 OF APOPROTEIN AND IN COMPLEXES WITH TNFRSF5 AND TNFRSF11A PEPTIDES, FUNCTION, SUBUNIT.
[55]"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.
[56]"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.
[57]"E2 interaction and dimerization in the crystal structure of TRAF6."
Yin Q., Lin S.C., Lamothe B., Lu M., Lo Y.C., Hura G., Zheng L., Rich R.L., Campos A.D., Myszka D.G., Lenardo M.J., Darnay B.G., Wu H.
Nat. Struct. Mol. Biol. 16:658-666(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7901.1.
PIRS71821.
RefSeqNP_004611.1. NM_004620.3.
NP_665802.1. NM_145803.2.
UniGeneHs.444172.
Hs.591983.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9Y4K3.
SMRQ9Y4K3. Positions 54-210, 302-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113041. 219 interactions.
DIPDIP-27515N.
IntActQ9Y4K3. 81 interactions.
MINTMINT-88585.
STRING9606.ENSP00000316840.

PTM databases

PhosphoSiteQ9Y4K3.

Polymorphism databases

DMDM30580642.

Proteomic databases

MaxQBQ9Y4K3.
PaxDbQ9Y4K3.
PRIDEQ9Y4K3.

Protocols and materials databases

DNASU7189.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348124; ENSP00000337853; ENSG00000175104.
ENST00000526995; ENSP00000433623; ENSG00000175104.
GeneID7189.
KEGGhsa:7189.
UCSCuc001mwq.2. human.

Organism-specific databases

CTD7189.
GeneCardsGC11M036467.
HGNCHGNC:12036. TRAF6.
HPACAB004605.
HPA019805.
HPA020599.
MIM602355. gene.
neXtProtNX_Q9Y4K3.
Orphanet1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
PharmGKBPA36713.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289765.
HOGENOMHOG000006625.
HOVERGENHBG060248.
InParanoidQ9Y4K3.
KOK03175.
OMANFQETIH.
OrthoDBEOG7966G5.
PhylomeDBQ9Y4K3.
TreeFamTF321154.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ9Y4K3.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9Y4K3.
CleanExHS_TRAF6.
GenevestigatorQ9Y4K3.

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:SF52. PTHR10131:SF52. 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

ChiTaRSTraf6. human.
EvolutionaryTraceQ9Y4K3.
GeneWikiTRAF6.
GenomeRNAi7189.
NextBio28192.
PROQ9Y4K3.
SOURCESearch...

Entry information

Entry nameTRAF6_HUMAN
AccessionPrimary (citable) accession number: Q9Y4K3
Secondary accession number(s): A6NKI7 expand/collapse secondary AC list , A8KAB3, D3DR16, Q8NEH5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM