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Protein Page:
TRAF6 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TRAF6 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. Homotrimer. Homooligomer. N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Binds to TNFRSF5/CD40 and TNFRSF11A/RANK. Associates with NGFR, TNFRSF17, IRAK1, IRAK2, IRAK3, IRAK4, 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. Interacts with PELI1, PELI2 and PELI3. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1. Interacts with IL1RL1. Interacts with TRAFD1. Interacts with ZNF675. Interacts with AJUBA. Interacts with TICAM1 and TICAM2. Interacts with ZFAND5. 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 (via TRAF domains) with WDR34 (via WD domains). Interacts with RBCK1. Interacts with TRAF3IP2. Interacts with LIMD1 (via LIM domains). Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Belongs to the TNF receptor-associated factor family. A subfamily. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Ubiquitin conjugating system; Ligase; EC 6.3.2.-
Cellular Component: cytoplasm; cytosol; internal side of plasma membrane; lipid particle; mitochondrion; nucleolus; nucleus; perinuclear region of cytoplasm; plasma membrane; protein complex
Molecular Function: histone deacetylase binding; identical protein binding; mitogen-activated protein kinase kinase kinase binding; protein binding; protein kinase B binding; protein kinase binding; protein N-terminus binding; signal transducer activity; thioesterase binding; tumor necrosis factor receptor binding; ubiquitin conjugating enzyme binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity
Biological Process: activation of NF-kappaB transcription factor; activation of NF-kappaB-inducing kinase; activation of protein kinase activity; antigen processing and presentation of exogenous peptide antigen via MHC class II; bone remodeling; bone resorption; cell development; cytokine and chemokine mediated signaling pathway; I-kappaB kinase/NF-kappaB cascade; immune response; JNK cascade; myeloid dendritic cell differentiation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; neural tube closure; odontogenesis of dentine-containing teeth; organ morphogenesis; ossification; osteoclast differentiation; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interleukin-12 biosynthetic process; positive regulation of interleukin-2 production; positive regulation of interleukin-6 biosynthetic process; positive regulation of JNK activity; positive regulation of lipopolysaccharide-mediated signaling pathway; positive regulation of osteoclast differentiation; positive regulation of smooth muscle cell proliferation; positive regulation of T cell cytokine production; positive regulation of T cell proliferation; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; protein autoubiquitination; protein complex assembly; protein polyubiquitination; protein ubiquitination; regulation of immunoglobulin secretion; signal transduction; T cell receptor signaling pathway; T-helper 1 type immune response
Reference #:  P70196 (UniProtKB)
Alt. Names/Synonyms: 2310003F17Rik; AI851288; C630032O20Rik; E3 ubiquitin-protein ligase TRAF6; OTTMUSP00000015480; RP23-313G3.1; TNF receptor-associated factor 6; Traf6
Gene Symbols: Traf6
Molecular weight: 60,070 Da
Basal Isoelectric point: 6.1  Predict pI for various phosphorylation states
CST Pathways:  NF-kB Signaling  |  Toll-Like Receptor Signaling
Select Structure to View Below

TRAF6

Protein Structure Not Found.
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Download ChimeraX Script


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Sites Implicated In
transcription, inhibited: T471‑p, T494‑p
protein conformation: T471‑p, T494‑p
ubiquitination: T471‑p, T494‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 S9‑p SLLNCENsCGssQsS
0 1 S12‑p NCENsCGssQsSSDC
0 1 S13‑p CENsCGssQsSSDCC
0 1 S15‑p NsCGssQsSSDCCAA
1 0 K124 LFPDNFAKREILSLT
0 2 S291‑p LRPCDAAsPSRGCRP
0 2 Y334 KMETQSMYVGELKRT
0 3 K339 SMYVGELKRTIRTLE
1 0 T471‑p LLAFQRPtIPRNPKG
1 1 T494‑p LEALRQGtFIKDDTL
0 1 T500 GtFIKDDTLLVRCEV
0 5 G515 STRFDMGGLRKEGFQ
  human

 
S9 SLLNCENSCGSSQSE
S12 NCENSCGSSQSESDC
S13 CENSCGSSQSESDCC
S15 NSCGSSQSESDCCVA
K124‑ub LFPDNFAkREILSLM
I283 AVHSLSVIPDSGYIS
Y326‑p KMETQSMyVSELkRT
K331‑ub SMyVSELkRTIRTLE
T463 LLAFQRPTIPRNPKG
T486‑p LEALRQRtFIKDDtL
T492‑p RtFIKDDtLLVRCEV
S507‑p STRFDMGsLRREGFQ
  rat

 
S9 SLLNCENSCASSQSS
S12 NCENSCASSQSSSDC
S13 CENSCASSQSSSDCC
S15 NSCASSQSSSDCCAA
K124 LFPDNFAKREILSLT
S291 LRPCDASSPSRGCRP
H334 KMETQSMHVSELKRT
K339 SMHVSELKRTIRSLE
T471 LLAFQRPTIPRNPKG
T494 LEALRQGTFIKDDTL
T500 GTFIKDDTLLVRCEV
G515 STRFDMGGLRKEGFQ
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