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Protein Page:
TNF-R1 (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TNF-R1 Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate- specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein. Interacts with human cytomegalovirus/HHV-5 protein UL138. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Receptor, cytokine; Membrane protein, integral
Cellular Component: Golgi membrane; Golgi apparatus; extracellular space; protein complex; cell surface; membrane; axon; integral to membrane; plasma membrane; intracellular; nucleus; receptor complex; lipid raft
Molecular Function: protein binding; tumor necrosis factor receptor activity; protease binding; protein complex binding; tumor necrosis factor binding
Biological Process: positive regulation of protein import into nucleus, translocation; apoptosis; protein heterooligomerization; cytokine and chemokine mediated signaling pathway; programmed cell death; defense response; positive regulation of tumor necrosis factor production; signal transduction; prostaglandin metabolic process; regulation of apoptosis; positive regulation of tyrosine phosphorylation of Stat1 protein; positive regulation of angiogenesis; cell surface receptor linked signal transduction; tumor necrosis factor-mediated signaling pathway; DNA damage response, signal transduction resulting in induction of apoptosis; negative regulation of inflammatory response; defense response to bacterium; negative regulation of interleukin-6 production; positive regulation of transcription from RNA polymerase II promoter; inflammatory response; negative regulation of apoptosis; positive regulation of inflammatory response
Reference #:  P25118 (UniProtKB)
Alt. Names/Synonyms: CD120a; FPF; OTTMUSP00000028139; p55; p55-R; p60; TNF receptor alpha chain; TNF-alpha-R1; TNF-alphaR1; TNF-R; TNF-R-I; TNF-R1; TNF-R55; TNF-RI; TNFalpha-R1; TNFAR; Tnfr-1; Tnfr-2; TNFR-I; Tnfr1; TNFR60; TNFRI; TNFRp55; Tnfrsf1a; TNR1A; Tumor necrosis factor receptor 1; Tumor necrosis factor receptor superfamily member 1A; tumor necrosis factor receptor superfamily, member 1a; Tumor necrosis factor receptor type I
Gene Symbols: Tnfrsf1a
Molecular weight: 50,130 Da
Basal Isoelectric point: 7.36  Predict pI for various phosphorylation states
CST Pathways:  Death Receptor Signaling  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  NF-kB Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TNF-R1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  Source  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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.


       mouse

 
0 1 R239-m1 SLMCRYPrWrPEVYS
0 1 R241-m1 MCRYPrWrPEVYSII
2 0 T265-p EKAGKPLtPAPsPAF
2 0 S269-p KPLtPAPsPAFsPTS
2 0 S273-p PAPsPAFsPTSGFNP
1 0 T286-p NPTLGFStPGFSsPV
1 0 S291-p FStPGFSsPVSStPI
1 0 T296-p FSsPVSStPIsPIFG
2 0 S299-p PVSStPIsPIFGPSN
0 7 T319 PVSEVVPTQGADPLL
1 1 Y360 NADLAILYAVVDGVP
1 0 S381 FMRFMGLSEHEIERL
1 6 Y401 RCLREAQYSMLEAWR
0 2 T417 RTPRHEDTLEVVGLV
  human

 
R238 GLMYRYQRWKSKLYS
K240 MYRYQRWKSKLYSIV
A268 GTTTKPLAPNPSFSP
- gap
S274 LAPNPSFSPTPGFTP
V288 PTLGFSPVPSSTFTS
F293 SPVPSSTFTSSSTYT
T298 STFTSSSTYTPGDCP
- gap
Y318-p RREVAPPyQGADPIL
Y360-p TDDPATLyAVVENVP
S381-p FVRRLGLsDHEIDRL
Y401-p RCLREAQySMLATWR
T417-p RTPRREAtLELLGRV
  rat

 
Q238 SLLCRYPQWRPRVYS
R240 LCRYPQWRPRVYSII
T268 GIVTKPLTPASIPAF
I272 KPLTPASIPAFSPNP
S276 PASIPAFSPNPGFNP
T290 PTLGFSTTPRFSHPV
H295 STTPRFSHPVSSTPI
T300 FSHPVSSTPISPVFG
S303 PVSSTPISPVFGPSN
T324 PVREVVPTQGADPLL
Y367 TADPAMLYAVVDGVP
S388 FMRLLGLSEHEIERL
Y408 RCLREAHYSMLEAWR
T424 RTPRHEATLDVVGRV
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