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Search results 501 to 600 out of 753 for Traf2

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Type Details Score
Publication
20184394 | -
First Author: Kanno Y
Year: 2010
Journal: J Recept Signal Transduct Res
Title: TACI induces cIAP1-mediated ubiquitination of NIK by TRAF2 and TANK to limit non-canonical NF-kappaB signaling.
Volume: 30
Issue: 2
Pages: 121-32
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Strain
MGI:5556770 | B6NTac;B6N-A<tm1Brd> Tnik<tm3a(EUCOMM)Wtsi>/WtsiBiat
Attribute String: mutant strain, targeted mutation
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Publication
19409903 | -
First Author: Zhang L
Year: 2009
Journal: J Mol Biol
Title: TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells.
Volume: 389
Issue: 3
Pages: 495-510
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Publication
18362156 | -
First Author: Yang CH
Year: 2008
Journal: J Biol Chem
Title: The role of TRAF2 binding to the type I interferon receptor in alternative NF kappaB activation and antiviral response.
Volume: 283
Issue: 21
Pages: 14309-16
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Genotype
Genotype
Symbol: Apc/Apc<+> Tnik/Tnik
Background: involves: C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Allele
Tg(H2-K/Igh-Traf2*)#Ywc | MGI:4850018
Name: transgene insertion, Yongwon Choi
Allele Type: Transgenic
Attribute String: Dominant negative, Inserted expressed sequence
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Protein Domain
IPR037305 | TRAF2_MATH
Type: Domain
Description: TNF receptor-associated factor 2 (TRAF2) regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis [, ].TRAF2 is heavily regulated by ubiquitin signals. It has E3 ubiquitin-protein ligase activity and promotes K63-linked ubiquitination of target proteins. Alternatively, TRAF2 may be required for recruiting other E3 ligases, such as A20, to help processing and turnover. Furthermore, TRAF2 is regulated by both K63 and K48 type ubiquitin chains. K63 linkage may be mediated by TRAF2 auto-ubiquitination, and is required for TRAF2 activation. c-IAPl and Siah2 are known E3 ligases that can K48-ubiquitinate TRAF2 to target it for proteasome-dependent degradation [, , ]. TRAF2 contains a RING finger domain, five zinc finger domains, and a TRAF domain. The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded β-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors [, ].
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Publication
19061864 | J:142909
First Author: Uechi Y
Year: 2009
Journal: Biochem Biophys Res Commun
Title: Rap2 function requires palmitoylation and recycling endosome localization.
Volume: 378
Issue: 4
Pages: 732-7
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Allele
Cyld<tm1.1Awai> | MGI:3761624
Name: CYLD lysine 63 deubiquitinase; targeted mutation 1.1, Ari Waisman
Allele Type: Targeted
Attribute String: Null/knockout
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Allele
Tradd<tm1.1Zgl> | MGI:3810080
Name: TNFRSF1A-associated via death domain; targeted mutation 1.1, Zhenggang Liu
Allele Type: Targeted
Attribute String: Null/knockout
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Publication
21421854 | J:172750
First Author: Pobezinskaya YL
Year: 2011
Journal: J Immunol
Title: The adaptor protein TRADD is essential for TNF-like ligand 1A/death receptor 3 signaling.
Volume: 186
Issue: 9
Pages: 5212-6
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Genotype
Genotype
Symbol: Cyld/Cyld
Background: Not Specified
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tradd/Tradd
Background: involves: C57BL/6 * FVB/N
Zygosity: hm
Has Mutant Allele: true
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Publication
17923499 | J:126113
First Author: Hövelmeyer N
Year: 2007
Journal: J Exp Med
Title: Regulation of B cell homeostasis and activation by the tumor suppressor gene CYLD.
Volume: 204
Issue: 11
Pages: 2615-27
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Publication
12887920 | J:341414
First Author: Micheau O
Year: 2003
Journal: Cell
Title: Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes.
Volume: 114
Issue: 2
Pages: 181-90
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Publication
18429822 | J:141705
First Author: Kato T Jr
Year: 2008
Journal: Genes Cells
Title: Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-mediated phosphorylation of TRAF1.
Volume: 13
Issue: 5
Pages: 509-20
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Publication
23690480 | J:204832
First Author: Martinez-Forero I
Year: 2013
Journal: J Immunol
Title: T cell costimulation with anti-CD137 monoclonal antibodies is mediated by K63-polyubiquitin-dependent signals from endosomes.
Volume: 190
Issue: 12
Pages: 6694-706
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Publication
18641653 | J:139031
First Author: Pobezinskaya YL
Year: 2008
Journal: Nat Immunol
Title: The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors.
Volume: 9
Issue: 9
Pages: 1047-54
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Publication
33912159 | J:314110
 
First Author: Perez-Chacon G
Year: 2021
Journal: Front Immunol
Title: The Traf2DNxBCL2-tg Mouse Model of Chronic Lymphocytic Leukemia/Small Lymphocytic Lymphoma Recapitulates the Biased IGHV Gene Usage, Stereotypy, and Antigen-Specific HCDR3 Selection of Its Human Counterpart.
Volume: 12
Pages: 627602
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Genotype
Genotype
Symbol: Tg(BCL2/IGH)#Jcre/? Tg(H2-K/Igh-Traf2*)#Ywc/?
Background: involves: BALB/c * C57BL/6 * CBA/J * FVB/N * SJL/J * SWR/J
Zygosity: cx
Has Mutant Allele: true
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Publication
19935683 | -
First Author: Kulathu Y
Year: 2009
Journal: Nat Struct Mol Biol
Title: Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain.
Volume: 16
Issue: 12
Pages: 1328-30
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Publication
17449468 | -
First Author: Tian Y
Year: 2007
Journal: J Biol Chem
Title: RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation.
Volume: 282
Issue: 23
Pages: 16776-82
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Publication
10882101 | -
First Author: Takaesu G
Year: 2000
Journal: Mol Cell
Title: TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway.
Volume: 5
Issue: 4
Pages: 649-58
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Publication
14633987 | -
First Author: Ishitani T
Year: 2003
Journal: EMBO J
Title: Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling.
Volume: 22
Issue: 23
Pages: 6277-88
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Protein Domain
IPR041911 | TAB2/3_CUE
Type: Domain
Description: TAB2 (TGF-beta-activated kinase 1 and MAP3K7-binding protein 2) is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway []. TAB3 is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2 []. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction []. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD) [].This entry represents the CUE domain found in TAB2 and TAB3.
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Protein
E0CX37
Organism: Mus musculus/domesticus
Length: 37  
Fragment?: true
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Publication
9325055 | -
First Author: Huang X
Year: 1997
Journal: Genomics
Title: Genomic organization of the human PP4 gene encoding a serine/threonine protein phosphatase (PP4) suggests a common ancestry with PP2A.
Volume: 44
Issue: 3
Pages: 336-43
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Publication
10769191 | -
 
First Author: Hastie CJ
Year: 2000
Journal: Biochem J
Title: A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres.
Volume: 347 Pt 3
Pages: 845-55
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Publication
10026142 | -
First Author: Kloeker S
Year: 1999
Journal: J Biol Chem
Title: Purification and identification of a novel subunit of protein serine/threonine phosphatase 4.
Volume: 274
Issue: 9
Pages: 5339-47
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Protein Domain
IPR031087 | PP4R1
Type: Family
Description: PP4R1 is a regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). The catalytic subunit of PP4 (PP4C) belongs to the PP2A family of serine/threonine protein phosphatases []. Although 65% identical to the catalytic subunit of PP2AC, PP4C does not associate with the regulatory subunit of PP2A. Instead, PP4C associates with two other regulatory subunits, PP4R1 []and PP4R2 [].PP4R1 targets TRAF2 and TRAF6 to mediate inhibition of NF-kB activation [].
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Publication
27824289 | J:318371
First Author: Ye A
Year: 2016
Journal: Epigenetics
Title: PEG3 binds to H19-ICR as a transcriptional repressor.
Volume: 11
Issue: 12
Pages: 889-900
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Publication
30741936 | J:275412
First Author: Dowling JP
Year: 2019
Journal: Nat Commun
Title: TRADD regulates perinatal development and adulthood survival in mice lacking RIPK1 and RIPK3.
Volume: 10
Issue: 1
Pages: 705
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Publication
27372382 | J:335031
 
First Author: Reuter S
Year: 2016
Journal: Cell Immunol
Title: Cylindromatosis (Cyld) gene mutation in T cells promotes the development of an IL-9-dependent allergic phenotype in experimental asthma.
Volume: 308
Pages: 27-34
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Publication
11098060 | -
First Author: Leo E
Year: 2001
Journal: J Biol Chem
Title: TRAF1 is a substrate of caspases activated during tumor necrosis factor receptor-alpha-induced apoptosis.
Volume: 276
Issue: 11
Pages: 8087-93
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Publication
9847406 | -
First Author: Wajant H
Year: 1998
Journal: J Mol Evol
Title: Identification of a TRAF (TNF receptor-associated factor) gene in Caenorhabditis elegans.
Volume: 47
Issue: 6
Pages: 656-62
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Publication
9744859 | -
First Author: Arch RH
Year: 1998
Journal: Genes Dev
Title: Tumor necrosis factor receptor-associated factors (TRAFs)--a family of adapter proteins that regulates life and death.
Volume: 12
Issue: 18
Pages: 2821-30
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Publication
10021364 | -
First Author: Liu H
Year: 1999
Journal: Curr Biol
Title: A Drosophila TNF-receptor-associated factor (TRAF) binds the ste20 kinase Misshapen and activates Jun kinase.
Volume: 9
Issue: 2
Pages: 101-4
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Protein
Q8C245
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Publication
10911999 | -
First Author: Tsao DH
Year: 2000
Journal: Mol Cell
Title: Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway.
Volume: 5
Issue: 6
Pages: 1051-7
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Publication
10650002 | J:132966
First Author: Urano F
Year: 2000
Journal: Science
Title: Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Volume: 287
Issue: 5453
Pages: 664-6
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Publication
8791485 | J:31795
First Author: Tewari M
Year: 1996
Journal: Curr Opin Genet Dev
Title: Recent advances in tumor necrosis factor and CD40 signaling.
Volume: 6
Issue: 1
Pages: 39-44
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Protein
F7AT87
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
D3Z216
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: true
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Protein Domain
IPR036729 | TRADD_N_sf
Type: Homologous_superfamily
Description: TRADD is a signalling adaptor protein involved in tumour necrosis factor-receptor I (TNFR1)-associated apoptosis and cell survival. The decision between apoptosis and cell survival involves the interplay between two sequential signalling complexes. The plasma membrane-bound complex I is comprised of TNFR1, TRADD, the kinase RIP1, and TRAF2, which together mediate the activation of NF-kappaB. Subsequently, complex II is formed in the cytoplasm, where TRADD and RIP1 associate with FADD and caspase-8. If NF-kappaB is activated by complex I, then complex II will associate with the caspase-8 inhibitor FLIP(L) and the cell survives, while the failure to activate NF-kappaB leads to apoptosis [].TRADD contains two functionally separate domains, which allow the protein to couple to two distinct signaling pathways. The TRADD C-terminal death domain is responsible for its association with TNFR1, and with the death-domain proteins FADD and RIP1, which promote apoptosis. The TRADD N-terminal domain binds TRAF2 and promotes TRAF2 recruitment to TNFR1, thereby mediating the activation of NK-kappaB and JNK/AP1, which promote cell survival []. The N-terminal TRADD domain is composed of an α/β sandwich, where the β-strands form an antiparallel β-sheet.
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Protein Domain
IPR009095 | TRADD_N
Type: Domain
Description: TRADD is a signalling adaptor protein involved in tumour necrosis factor-receptor I (TNFR1)-associated apoptosis and cell survival. The decision between apoptosis and cell survival involves the interplay between two sequential signalling complexes. The plasma membrane-bound complex I is comprised of TNFR1, TRADD, the kinase RIP1, and TRAF2, which together mediate the activation of NF-kappaB. Subsequently, complex II is formed in the cytoplasm, where TRADD and RIP1 associate with FADD and caspase-8. If NF-kappaB is activated by complex I, then complex II will associate with the caspase-8 inhibitor FLIP(L) and the cell survives, while the failure to activate NF-kappaB leads to apoptosis [].TRADD contains two functionally separate domains, which allow the protein to couple to two distinct signaling pathways. The TRADD C-terminal death domain is responsible for its association with TNFR1, and with the death-domain proteins FADD and RIP1, which promote apoptosis. The TRADD N-terminal domain binds TRAF2 and promotes TRAF2 recruitment to TNFR1, thereby mediating the activation of NK-kappaB and JNK/AP1, which promote cell survival []. The N-terminal TRADD domain is composed of an α/β sandwich, where the β-strands form an antiparallel β-sheet.
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Protein Domain
IPR012227 | TNF_rcpt-assoc_TRAF_met
Type: Family
Description: The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals []. TRAFs constitute a family of genetically conserved adapter proteins found in mammals (TRAF1-6) as well as in other multicellular organisms such as Drosophila [], Caenorhabditis elegans []. TRAF2 is the prototypical member of the family. Mammalian TRAF1 and TRAF2 were the first members initially identified by their association with TNFR2. The TRAF1/TRAF2 and TRAF3/TRAF5 gene pairs may have arisen from recent independent gene duplications and to share a common ancestral gene. TRAF4 and TRAF6 precursor genes may have arisen earlier during evolution, with the divergence of the TRAF6 precursor occurring earliest of all. Except TRAF1, this PIRSF has a general domain architecture containing one N-terminal RING finger, a variable number of middle region of TRAF-type zinc finger and C2H2 type of zinc finger, and one C-terminal MATH domain. TRAF1 is unique in the family in that it lacks the N-terminal RING and zinc-finger domains []. This has rendered TRAF1 unable to promote TNF receptor signalling and act as a "dominant negative"TRAF []. Also TRAF1 is a substrate for caspases activated by TNF family death receptors []. The larger C-terminal cleaved fragment can bind to and sequester TRAF2 from TNFR1 complex, therefore modulating TNF induced NFkB activation []. A wide range of biological functions, such as adaptive and innate immunity, embryonic development, stress response and bone metabolism, are mediated by TRAFs through the induction of cell survival, proliferation, differentiation and death. TRAFs are functionally divergent from a perspective of both upstream and downstream TRAF signal transduction pathways and of signalling-dependent regulation of TRAF trafficking. Each TRAF protein interacts with and mediates the signal transduction of multiple receptors, and in turn each receptor utilises multiple TRAFs for specific functions []. About 40 interaction partners of TRAF have been described thus far, including receptors, kinases, regulators and adaptor proteins.TRAF proteins can be recruited to and activated by ligand-engaged receptors in least three distinct ways []. 1) Members of the TNFR superfamily that do not contain intracellular death domains, such as TNFR2 and CD40, recruit TRAFs directly via short sequences in their intracellular tails []. 2) Those that contain an intracellular death domain, such as TNFR1, first recruit an adapter protein, TRADD, via a death-domain-death-domain interaction, which then serves as a central platform of the TNFR1 signalling complex, which assembles TRAF2 and RIP for survival signalling, and FADD and caspase-8 for the induction of apoptosis. 3) Members of the IL-1R/TLR superfamily contain a protein interaction module known as the TIR domain, which recruits, sequentially, MyD88, a TIR domain and death domain containing protein, and IRAKs, adapter Ser/Thr kinases with death domains. IRAKs in turn associate with TRAF6 to elicit signalling by IL-1 and pathogenic components such as LPS. A common mechanism for the membrane-proximal event in TRAF signalling has been revealed by the conserved trimeric association in the crystal structure of the TRAF domain of TRAF2 [].This entry represents the TNF receptor associated factors found in metazoa.
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Protein Domain
IPR043211 | TNF_rcpt-assoc_TRAF
Type: Family
Description: The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals []. TRAFs constitute a family of genetically conserved adapter proteinsfound in mammals (TRAF1-6) as well as in other multicellular organisms such as Drosophila [], Caenorhabditis elegans []. TRAF2 is the prototypical member of the family. Mammalian TRAF1 and TRAF2 were the first members initially identified by their association with TNFR2. The TRAF1/TRAF2 and TRAF3/TRAF5 gene pairs may have arisen from recent independent gene duplications and to share a common ancestral gene. TRAF4 and TRAF6 precursor genes may have arisen earlier during evolution, with the divergence of the TRAF6 precursor occurring earliest of all. Except TRAF1, this PIRSF has a general domain architecture containing one N-terminal RING finger, a variable number of middle region of TRAF-type zinc finger and C2H2 type of zinc finger, and one C-terminal MATH domain. TRAF1 is unique in the family in that it lacks the N-terminal RING and zinc-finger domains []. This has rendered TRAF1 unable to promote TNF receptor signalling and act as a "dominant negative"TRAF []. Also TRAF1 is a substrate for caspases activated by TNF family death receptors []. The larger C-terminal cleaved fragment can bind to and sequester TRAF2 from TNFR1 complex, therefore modulating TNF induced NFkB activation []. A wide range of biological functions, such as adaptive and innate immunity, embryonic development, stress response and bone metabolism, are mediated by TRAFs through the induction of cell survival, proliferation, differentiation and death. TRAFs are functionally divergent from a perspective of both upstream and downstream TRAF signal transduction pathways and of signalling-dependent regulation of TRAF trafficking. Each TRAF protein interacts with and mediates the signal transduction of multiple receptors, and in turn each receptor utilises multiple TRAFs for specific functions []. About 40 interaction partners of TRAF have been described thus far, including receptors, kinases, regulators and adaptor proteins.TRAF proteins can be recruited to and activated by ligand-engaged receptors in least three distinct ways []. 1) Members of the TNFR superfamily that do not contain intracellular death domains, such as TNFR2 and CD40, recruit TRAFs directly via short sequences in their intracellular tails []. 2) Those that contain an intracellular death domain, such as TNFR1, first recruit an adapter protein, TRADD, via a death-domain-death-domain interaction, which then serves as a central platform of the TNFR1 signalling complex, which assembles TRAF2 and RIP for survival signalling, and FADD and caspase-8 for the induction of apoptosis. 3) Members of the IL-1R/TLR superfamily contain a protein interaction module known as the TIR domain, which recruits, sequentially, MyD88, a TIR domain and death domain containing protein, and IRAKs, adapter Ser/Thr kinases with death domains. IRAKs in turn associate with TRAF6 to elicit signalling by IL-1 and pathogenic components such as LPS. A common mechanism for the membrane-proximal event in TRAF signalling has been revealed by the conserved trimeric association in the crystal structure of the TRAF domain of TRAF2 [].
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Publication
11865024 | -
First Author: Chung JY
Year: 2002
Journal: J Cell Sci
Title: All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction.
Volume: 115
Issue: Pt 4
Pages: 679-88
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Protein
P39428
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q3UM74
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q4VA12
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Publication
23066153 | J:190708
First Author: Reissig S
Year: 2012
Journal: J Immunol
Title: The tumor suppressor CYLD controls the function of murine regulatory T cells.
Volume: 189
Issue: 10
Pages: 4770-6
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Publication
19342479 | J:149355
First Author: Srokowski CC
Year: 2009
Journal: Blood
Title: Naturally occurring short splice variant of CYLD positively regulates dendritic cell function.
Volume: 113
Issue: 23
Pages: 5891-5
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Publication
25675948 | J:229783
First Author: Wurm R
Year: 2015
Journal: Eur J Immunol
Title: Protective dendritic cell responses against listeriosis induced by the short form of the deubiquitinating enzyme CYLD are inhibited by full-length CYLD.
Volume: 45
Issue: 5
Pages: 1366-76
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Publication
10206649 | -
First Author: Park YC
Year: 1999
Journal: Nature
Title: Structural basis for self-association and receptor recognition of human TRAF2.
Volume: 398
Issue: 6727
Pages: 533-8
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Publication
- | J:104190
     
First Author: The Australian Phenomics Facility at The Australian National University
Year: 2006
Journal: MGI Direct Data Submission
Title: Heritable mouse mutants from the ENU mutagenesis program at the Australian Phenomics Facility at The Australian National University
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Protein Domain
IPR037306 | TRAF1_MATH
Type: Domain
Description: TNF receptor-associated factor 1 (TRAF1) plays a role in the regulation of cell survival and apoptosis []. TRAF1 is unique among TRAF proteins in that it lacks a RING domain found in the N-terminal regions of other TRAFs []. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14 [, ].TRAF1 is unique among the TRAFs in that it lacks a RING domain, which is critical for the activation of nuclear factor-kappaB and Jun NH2-terminal kinase. Studies on TRAF1-deficient mice suggest that TRAF1 has a negative regulatory role in TNFR-mediated signaling events []. TRAF1 contains one zinc finger and one TRAF domain.The TRAF domain can be divided into a more divergent N-terminal alpha helical region (TRAF-N), and a highly conserved C-terminal MATH subdomain (TRAF-C) with an eight-stranded β-sandwich structure. TRAF-N mediates trimerization while TRAF-C interacts with receptors [, ].
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Protein Domain
IPR027136 | TRAF1
Type: Family
Description: TNF receptor-associated factor 1 (TRAF1) plays a role in the regulation of cell survival and apoptosis []. TRAF1 is unique among TRAF proteins in that it lacks a RING domain found in the N-terminal regions of other TRAFs []. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14 [, ].TRAF1 is unique among the TRAFs in that it lacks a RING domain, which is critical for the activation of nuclear factor-kappaB and Jun NH2-terminal kinase. Studies on TRAF1-deficient mice suggest that TRAF1 has a negative regulatory role in TNFR-mediated signaling events []. TRAF1 contains one zinc finger and one TRAF domain.
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Publication
16713561 | J:108769
First Author: Massoumi R
Year: 2006
Journal: Cell
Title: Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-kappaB signaling.
Volume: 125
Issue: 4
Pages: 665-77
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Publication
7533327 | J:34086
First Author: Cheng G
Year: 1995
Journal: Science
Title: Involvement of CRAF1, a relative of TRAF, in CD40 signaling.
Volume: 267
Issue: 5203
Pages: 1494-8
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Publication
22184250 | J:180128
First Author: Liu J
Year: 2012
Journal: Proc Natl Acad Sci U S A
Title: Site-specific ubiquitination is required for relieving the transcription factor Miz1-mediated suppression on TNF-α-induced JNK activation and inflammation.
Volume: 109
Issue: 1
Pages: 191-6
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Publication
10215628 | J:54467
First Author: Lomaga MA
Year: 1999
Journal: Genes Dev
Title: TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling.
Volume: 13
Issue: 8
Pages: 1015-24
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Publication
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Protein
I6L995
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Fragment?: false
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Protein
D6RCI0
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Fragment?: false
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Protein
Q3U0V2
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Fragment?: false
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Protein
B2RRZ7
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Fragment?: false
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