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UniProtKB - Q9Y4K3 (TRAF6_HUMAN)

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Protein

TNF receptor-associated factor 6

Gene

TRAF6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein 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)DescriptionActionsGraphical viewLength
Zinc fingeri70 – 109RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri150 – 202TRAF-type 1PROSITE-ProRule annotationAdd BLAST53
Zinc fingeri203 – 259TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • 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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionTransferase
Biological processDNA damage, Immunity, Osteogenesis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-166058 MyD88:Mal cascade initiated on plasma membrane
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-193692 Regulated proteolysis of p75NTR
R-HSA-202424 Downstream TCR signaling
R-HSA-205043 NRIF signals cell death from the nucleus
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-9014325 TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-937041 IKK complex recruitment mediated by RIP1
R-HSA-937042 IRAK2 mediated activation of TAK1 complex
R-HSA-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975155 MyD88 dependent cascade initiated on endosome
R-HSA-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-HSA-975871 MyD88 cascade initiated on plasma membrane
SignaLinkiQ9Y4K3
SIGNORiQ9Y4K3
UniPathwayiUPA00143

Protein family/group databases

MoonDBiQ9Y4K3 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 6 (EC:2.3.2.27)
Alternative name(s):
E3 ubiquitin-protein ligase TRAF6
Interleukin-1 signal transducer
RING finger protein 85
RING-type E3 ubiquitin transferase TRAF6Curated
Gene namesi
Name:TRAF6
Synonyms:RNF85
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000175104.14
HGNCiHGNC:12036 TRAF6
MIMi602355 gene
neXtProtiNX_Q9Y4K3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi57D → K: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi70C → A: Loss of ligase activity, autoubiquitination and signaling capacity. 2 Publications1
Mutagenesisi72I → D: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi74L → E or K: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi88R → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-122. 1 Publication1
Mutagenesisi118F → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi118F → W: Partially impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi118F → Y: Partially impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi122F → A: Loss of TRAF6 homodimerization and partially impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-88. 1 Publication1
Mutagenesisi124K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 3 Publications1
Mutagenesisi142K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication1
Mutagenesisi453K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication1

Organism-specific databases

DisGeNETi7189
MalaCardsiTRAF6
OpenTargetsiENSG00000175104
Orphaneti1810 Autosomal dominant hypohidrotic ectodermal dysplasia
PharmGKBiPA36713

Chemistry databases

ChEMBLiCHEMBL3588728

Polymorphism and mutation databases

BioMutaiTRAF6
DMDMi30580642

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000564071 – 522TNF receptor-associated factor 6Add BLAST522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

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. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappaB signaling upon DNA damage (PubMed:25861989).7 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9Y4K3
MaxQBiQ9Y4K3
PaxDbiQ9Y4K3
PeptideAtlasiQ9Y4K3
PRIDEiQ9Y4K3
ProteomicsDBi86225

PTM databases

iPTMnetiQ9Y4K3
PhosphoSitePlusiQ9Y4K3

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000175104
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 TICAM2. Interacts with CARD14. Interacts with CD40 and MAP3K8; the interaction is required for ERK activation (By similarity). Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with TANK; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with USP10; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with ZC3H12A; this interaction increases in response to DNA damage and is stimulated by TANK (PubMed:25861989). Interacts with WDFY3 (By similarity). Interacts with TRIM13 (PubMed:28087809). Interacts with GPS2 (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • 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 binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113041, 301 interactors
CORUMiQ9Y4K3
DIPiDIP-27515N
ELMiQ9Y4K3
IntActiQ9Y4K3, 113 interactors
MINTiQ9Y4K3
STRINGi9606.ENSP00000337853

Chemistry databases

BindingDBiQ9Y4K3

Structurei

Secondary structure

1522
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 62Combined sources3
Helixi66 – 68Combined sources3
Turni71 – 73Combined sources3
Beta strandi78 – 82Combined sources5
Turni84 – 86Combined sources3
Beta strandi88 – 90Combined sources3
Helixi91 – 101Combined sources11
Turni106 – 108Combined sources3
Helixi114 – 116Combined sources3
Helixi121 – 128Combined sources8
Beta strandi130 – 133Combined sources4
Beta strandi135 – 138Combined sources4
Beta strandi142 – 144Combined sources3
Helixi145 – 147Combined sources3
Helixi149 – 151Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi158 – 161Combined sources4
Turni163 – 165Combined sources3
Beta strandi168 – 170Combined sources3
Helixi171 – 173Combined sources3
Helixi174 – 180Combined sources7
Beta strandi186 – 188Combined sources3
Turni190 – 192Combined sources3
Beta strandi195 – 197Combined sources3
Helixi198 – 200Combined sources3
Helixi201 – 205Combined sources5
Beta strandi351 – 357Combined sources7
Helixi360 – 368Combined sources9
Beta strandi373 – 376Combined sources4
Beta strandi380 – 385Combined sources6
Beta strandi388 – 395Combined sources8
Turni401 – 405Combined sources5
Beta strandi406 – 414Combined sources9
Helixi419 – 421Combined sources3
Beta strandi428 – 434Combined sources7
Helixi440 – 442Combined sources3
Beta strandi446 – 451Combined sources6
Helixi457 – 459Combined sources3
Beta strandi463 – 466Combined sources4
Beta strandi468 – 478Combined sources11
Helixi479 – 483Combined sources5
Turni484 – 486Combined sources3
Beta strandi492 – 500Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Z8MX-ray2.95A/B346-504[»]
ProteinModelPortaliQ9Y4K3
SMRiQ9Y4K3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y4K3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini350 – 499MATHPROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 354Interaction with TAX1BP11 PublicationAdd BLAST354
Regioni355 – 522Interaction with TANK1 PublicationAdd BLAST168

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili288 – 348Sequence analysisAdd BLAST61

Domaini

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

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri70 – 109RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri150 – 202TRAF-type 1PROSITE-ProRule annotationAdd BLAST53
Zinc fingeri203 – 259TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ISDW Eukaryota
ENOG410XTXK LUCA
GeneTreeiENSGT00550000074359
HOGENOMiHOG000006625
HOVERGENiHBG060248
InParanoidiQ9Y4K3
KOiK03175
OMAiPGYKLCL
OrthoDBiEOG091G0GHD
PhylomeDBiQ9Y4K3
TreeFamiTF321154

Family and domain databases

CDDicd03776 MATH_TRAF6, 1 hit
Gene3Di2.60.210.10, 1 hit
3.30.40.10, 3 hits
InterProiView protein in InterPro
IPR002083 MATH/TRAF_dom
IPR012227 TNF_rcpt--assoc_TRAF
IPR008974 TRAF-like
IPR027139 TRAF6
IPR037309 TRAF6_MATH
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
IPR001293 Znf_TRAF
PANTHERiPTHR10131:SF111 PTHR10131:SF111, 1 hit
PfamiView protein in Pfam
PF02176 zf-TRAF, 1 hit
PIRSFiPIRSF015614 TRAF, 1 hit
SMARTiView protein in SMART
SM00061 MATH, 1 hit
SM00184 RING, 1 hit
SUPFAMiSSF49599 SSF49599, 3 hits
PROSITEiView protein in PROSITE
PS50144 MATH, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
PS50145 ZF_TRAF, 2 hits

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)DescriptionActionsGraphical viewLength
Sequence conflicti12S → F in AAH31052 (PubMed:15489334).Curated1

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.3 human

Similar proteinsi

Entry informationi

Entry nameiTRAF6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4K3
Secondary accession number(s): A6NKI7
, A8KAB3, D3DR16, Q8NEH5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1999
Last modified: June 20, 2018
This is version 206 of the entry and version 1 of the sequence. See 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

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