Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
TRAF2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TRAF2 Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'- linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin- protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Homotrimer, and heterotrimer with TRAF1 and TRAF3 (via TRAF domain). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro). Interacts with TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, CD27/TNFRSF7, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1 and IL15RA. Interacts with CDK9, CSK, MAP3K1, MAP3K5, MAP3K11, MAP3K14, MAP4K2, RIPK1, RIPK2, TNIK, TBK1, SPHK1, TRADD, TRAFD1, TRAIP, TANK/ITRAF, TNFAIP3, TDP2, MAVS/IPS1, TICAM1 and TRPC4AP. Interacts with CASP8AP2, NFATC2IP, PEG3 and HIVEP3. Interacts with BIRC2 and BIRC3 N- terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer. Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3. Interaction with BIRC2 and/or BIRC3 is essential for degradation of NFKBIA and activation of NF-kappa-B. Interacts with CYLD, USP48, DAB2IP, IKKA and IKKB. Identified in a complex with TNFRSF1A, RIPK1 and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3. Interacts with ERN1 and TAOK3. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1- phosphate. Belongs to the TNF receptor-associated factor family. A subfamily. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Autophagy; Ligase; EC 6.3.2.-; Ubiquitin ligase; Ubiquitin conjugating system
Cellular Component: internal side of plasma membrane; cytoplasm; cell cortex; cytosol; lipid raft
Molecular Function: sphingolipid binding; identical protein binding; zinc ion binding; CD40 receptor binding; ubiquitin-protein ligase activity; mitogen-activated protein kinase kinase kinase binding; tumor necrosis factor receptor binding; protein phosphatase binding; signal transducer activity; protein binding; enzyme binding; ubiquitin protein ligase binding; thioesterase binding; protein complex binding; ligase activity
Biological Process: caspase activation; positive regulation of JNK activity; protein autoubiquitination; apoptosis; protein heterooligomerization; activation of NF-kappaB-inducing kinase; positive regulation of T cell cytokine production; signal transduction; activation of NF-kappaB transcription factor; regulation of apoptosis; cellular protein complex assembly; tumor necrosis factor-mediated signaling pathway; positive regulation of interleukin-2 production; innate immune response; protein complex assembly; positive regulation of transcription factor activity; protein catabolic process; positive regulation of T cell activation; regulation of immunoglobulin secretion
Reference #:  Q12933 (UniProtKB)
Alt. Names/Synonyms: MGC:45012; TNF receptor-associated factor 2; TRAF2; TRAP; TRAP3; tumor necrosis factor type 2 receptor associated protein 3; Tumor necrosis factor type 2 receptor-associated protein 3
Gene Symbols: TRAF2
Molecular weight: 55,859 Da
Basal Isoelectric point: 7.66  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  Inhibition of Apoptosis  |  NF-kB Signaling  |  Regulation of P38 MAPKs  |  SAPK/JNK Signaling Cascades
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TRAF2

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
apoptosis, inhibited: S11‑p, S55‑p
activity, induced: T117‑p
molecular association, regulation: S11‑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


 SS 

SS: 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.


 MS 

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


       human

 
0 2 S5-p ___MAAAsVtPPGsL
0 4 T7-p _MAAAsVtPPGsLEL
0 2 P8 MAAAsVtPPGsLELL
3 5 S11-p AsVtPPGsLELLQPG
1 0 K21 LLQPGFSKtLLGtkL
0 1 T22-p LQPGFSKtLLGtkLE
0 1 T26-p FSKtLLGtkLEAKYL
0 8 K27-ub SKtLLGtkLEAKYLC
2 0 K31 LGtkLEAKYLCSACR
1 0 R38 KYLCSACRNVLRRPF
1 0 S55-p QCGHRYCsFCLASIL
0 1 S102-p AARREVEsLPAVCPS
2 0 T117-p DGCTWKGtLKEyESC
0 1 Y121-p WKGtLKEyESCHEGR
0 6 K140-ub LTECPACkGLVRLGE
0 12 K176-ub PCCGADVkAHHEVCP
0 48 K255-ub LSSVLEAkPLLGDQS
0 2 S274-p ELLQRCEsLEKKTAT
0 4 K313-ub QHRLDQDkIEALSSk
0 3 K320-ub kIEALSSkVQQLERS
0 4 K331-ub LERSIGLkDLAMADL
0 2 T401-p IYLNGDGtGRGTHLS
0 1 T431-p WPFNQKVtLMLLDQN
0 13 K481-ub PVSKMEAkNSYVRDD
13908 : Phospho-TRAF2 (Ser11) (E2B6L) Rabbit mAb
  mouse

 
S5 ___MAAASVTsPGSL
T7 _MAAASVTsPGSLEL
S8-p MAAASVTsPGSLELL
S11 ASVTsPGSLELLQPG
K21-ub LLQPGFSkTLLGTRL
T22 LQPGFSkTLLGTRLE
T26 FSkTLLGTRLEAkYL
R27 SkTLLGTRLEAkYLC
K31-ub LGTRLEAkYLCSACk
K38-ub kYLCSACkNILRRPF
S55 QCGHRYCSFCLTSIL
S102 AARREVESLPAVCPN
T117-p DGCTWKGtLKEYESC
Y121 WKGtLKEYESCHEGL
K140 LTECPACKGLVRLSE
E176 PCSHVDLEVHYEVCP
Q255 LSSFLEAQASPGTLN
I274 ELLQRCQILEQKIAT
K313 QHRLDQDKIEALSNK
K320 KIEALSNKVQQLERS
K331 LERSIGLKDLAMADL
T401 VYLNGDGTGRGTHLS
T431 WPFNQKVTLMLLDHN
K481 PVSKMEAKNSYVRDD
13908 : Phospho-TRAF2 (Ser11) (E2B6L) Rabbit mAb
  rat

 
S5 ___MAAASVTsPGSL
T7 _MAAASVTsPGSLEL
S8-p MAAASVTsPGSLELL
S11 ASVTsPGSLELLQPG
K21 LLQPGFSKTLLGTRL
T22 LQPGFSKTLLGTRLE
T26 FSKTLLGTRLEAKYL
R27 SKTLLGTRLEAKYLC
K31 LGTRLEAKYLCSACR
R38 KYLCSACRNILRRPF
S55 QCGHRYCSFCLTSIL
S102 AARREVESLPAVCPN
T117 DGCTWKGTLKEYESC
Y121 WKGTLKEYESCHEGL
K140 LTECPACKGLVRLSE
E176 PCSHADLELHYEVCP
Q254 LSSFLESQASQNQVG
I270 ELLQRCQILEQKIAT
K309 QHRLDQDKIEALSNK
K316 KIEALSNKVQQLERS
K327 LERSIGLKDLAMADL
T397 VYLNGDGTGRGTHLS
T427 WPFNQKVTLMLLDHN
K477 PVSKIEAKNSYVRDD
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.