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Protein

TNF receptor-associated factor 6

Gene

TRAF6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

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

  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
  • protein kinase B binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • thioesterase binding Source: UniProtKB
  • tumor necrosis factor receptor binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: MGI
  • ubiquitin protein ligase activity Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

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_188323. CLEC7A (Dectin-1) signaling.
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 Componenti: 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

  • CD40 receptor complex Source: BHF-UCL
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytosol Source: Reactome
  • endosome membrane Source: Reactome
  • lipid particle Source: UniProtKB
  • mitochondrion Source: HPA
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiTRAF6.
DMDMi30580642.

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.
GenevisibleiQ9Y4K3. HS.

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
itself3EBI-359276,EBI-359276
Q8V2D13EBI-359276,EBI-8622036From a different organism.
CD40P259422EBI-359276,EBI-525714
EcsitQ9QZH62EBI-359276,EBI-527020From a different organism.
EDARADDQ8WWZ35EBI-359276,EBI-2949647
IL1R1P147782EBI-359276,EBI-525905
IRAK1P516172EBI-359276,EBI-358664
MALT1Q9UDY83EBI-359276,EBI-1047372
MAP3K14Q995582EBI-359276,EBI-358011
MAP3K7O433182EBI-359276,EBI-358684
MEOX2A4D1273EBI-359276,EBI-10172134
NgfrP071742EBI-359276,EBI-1038810From a different organism.
PLEKHF2Q9H8W43EBI-359276,EBI-742388
POLIQ9UNA43EBI-359276,EBI-741774
RUSC1Q9BVN2-22EBI-359276,EBI-6257338
SPHK1Q9NYA12EBI-359276,EBI-985303
SQSTM1Q135012EBI-359276,EBI-307104
TAX1BP1Q86VP18EBI-359276,EBI-529518
TRAF1Q130778EBI-359276,EBI-359224
TRAF2Q129336EBI-359276,EBI-355744
TRAF3IP2O437344EBI-359276,EBI-744798
TRAF5O004638EBI-359276,EBI-523498
UBCP0CG483EBI-359276,EBI-3390054
UBE2D1P516682EBI-359276,EBI-743540
UBE2D2P628372EBI-359276,EBI-347677
UBE2D3P610772EBI-359276,EBI-348268
UBE2NP610883EBI-359276,EBI-1052908
USP2O756043EBI-359276,EBI-743272
VACWR178Q012202EBI-359276,EBI-3863691From a different organism.
VPS52Q8N1B43EBI-359276,EBI-2799833
XIAPP981702EBI-359276,EBI-517127
YES1P079473EBI-359276,EBI-515331
ZNF675Q8TD234EBI-359276,EBI-528190

Protein-protein interaction databases

BioGridi113041. 239 interactions.
DIPiDIP-27515N.
IntActiQ9Y4K3. 91 interactions.
MINTiMINT-88585.
STRINGi9606.ENSP00000337853.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074359.
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

« Hide

        10         20         30         40         50
MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM
60 70 80 90 100
EEIQGYDVEF DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD
110 120 130 140 150
AGHKCPVDNE ILLENQLFPD NFAKREILSL MVKCPNEGCL HKMELRHLED
160 170 180 190 200
HQAHCEFALM DCPQCQRPFQ KFHINIHILK DCPRRQVSCD NCAASMAFED
210 220 230 240 250
KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI PCTFSTFGCH
260 270 280 290 300
EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH
310 320 330 340 350
QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN
360 370 380 390 400
GIYIWKIGNF GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA
410 420 430 440 450
QRCANYISLF VHTMQGEYDS HLPWPFQGTI RLTILDQSEA PVRQNHEEIM
460 470 480 490 500
DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE ALRQRTFIKD DTLLVRCEVS
510 520
TRFDMGSLRR EGFQPRSTDA GV
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:
EMBLi
GenBanki
DDBJi
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.

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi113041. 239 interactions.
DIPiDIP-27515N.
IntActiQ9Y4K3. 91 interactions.
MINTiMINT-88585.
STRINGi9606.ENSP00000337853.

PTM databases

PhosphoSiteiQ9Y4K3.

Polymorphism and mutation databases

BioMutaiTRAF6.
DMDMi30580642.

Proteomic databases

MaxQBiQ9Y4K3.
PaxDbiQ9Y4K3.
PRIDEiQ9Y4K3.

Protocols and materials databases

DNASUi7189.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7189.
GeneCardsiGC11M036467.
HGNCiHGNC:12036. TRAF6.
HPAiCAB004605.
HPA019805.
HPA020599.
MIMi602355. gene.
neXtProtiNX_Q9Y4K3.
Orphaneti1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
PharmGKBiPA36713.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289765.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000006625.
HOVERGENiHBG060248.
InParanoidiQ9Y4K3.
KOiK03175.
OMAiNFQETIH.
OrthoDBiEOG7966G5.
PhylomeDBiQ9Y4K3.
TreeFamiTF321154.

Enzyme and pathway databases

UniPathwayiUPA00143.
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_188323. CLEC7A (Dectin-1) signaling.
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.

Miscellaneous databases

ChiTaRSiTRAF6. human.
EvolutionaryTraceiQ9Y4K3.
GeneWikiiTRAF6.
GenomeRNAii7189.
NextBioi28192.
PROiQ9Y4K3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y4K3.
CleanExiHS_TRAF6.
GenevisibleiQ9Y4K3. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 173 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.