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Search results 201 to 269 out of 269 for Traf1

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Type Details Score
Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
10499814 | J:57050
First Author: Dunn IF
Year: 1999
Journal: Mol Immunol
Title: Structure of the murine TRAF1 gene.
Volume: 36
Issue: 9
Pages: 611-7
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Strain
MGI:3767642 | C.129S4-Traf1<tm1Tsi>/TsiPryhJ
Attribute String: congenic, mutant strain, targeted mutation
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Allele
Traf1<em1Smoc> | MGI:7292944
Name: TNF receptor-associated factor 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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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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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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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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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
8643514 | J:33039
First Author: Uren AG
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors.
Volume: 93
Issue: 10
Pages: 4974-8
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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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Publication
11607847 | -
First Author: Bradley JR
Year: 2001
Journal: Oncogene
Title: Tumor necrosis factor receptor-associated factors (TRAFs).
Volume: 20
Issue: 44
Pages: 6482-91
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Publication
9461607 | J:45796
First Author: Brink R
Year: 1998
Journal: J Biol Chem
Title: Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended RING finger domain that inhibits TNFR2-mediated NF-kappaB activation.
Volume: 273
Issue: 7
Pages: 4129-34
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Publication
28747670 | J:253027
First Author: Alharshawi K
Year: 2017
Journal: Sci Rep
Title: PKC-ѳ is dispensable for OX40L-induced TCR-independent Treg proliferation but contributes by enabling IL-2 production from effector T-cells.
Volume: 7
Issue: 1
Pages: 6594
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Publication
15545599 | J:94116
First Author: Zapata JM
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: TNF receptor-associated factor (TRAF) domain and Bcl-2 cooperate to induce small B cell lymphoma/chronic lymphocytic leukemia in transgenic mice.
Volume: 101
Issue: 47
Pages: 16600-5
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Publication
15494504 | J:93747
First Author: Xie P
Year: 2004
Journal: J Immunol
Title: Roles of TNF receptor-associated factor 3 in signaling to B lymphocytes by carboxyl-terminal activating regions 1 and 2 of the EBV-encoded oncoprotein latent membrane protein 1.
Volume: 173
Issue: 9
Pages: 5546-55
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Publication
24798100 | J:217576
First Author: Zhu F
Year: 2014
Journal: Exp Cell Res
Title: The nuclear factor kappa B (NF-κB) activation is required for phagocytosis of staphylococcus aureus by RAW 264.7 cells.
Volume: 327
Issue: 2
Pages: 256-63
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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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Protein
A0A0A6YXC4
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Publication
10518213 | J:57751
First Author: Ye H
Year: 1999
Journal: Mol Cell
Title: The structural basis for the recognition of diverse receptor sequences by TRAF2.
Volume: 4
Issue: 3
Pages: 321-30
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Protein Domain
IPR001293 | Znf_TRAF
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found inclusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents TRAF-type zinc finger domains. Some of the proteins that have this domain are mammalian signal transducers associated with the cytoplasmic domain of the 75kDa tumour necrosis factor receptor []. A heterocomplex, homodimer or heterodimer of TRAF1 and TRAF2, binds to the N-terminal of the inhibitor of apoptosis proteins 1 and 2 (IAPS) and recruits them to the tumour necrosis factor receptor 2. Other proteins containing this domain include F45G2.6 protein from Caenorhabditis elegans and DG17 protein from Dictyostelium discoideum (Slime mold).
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Protein
P70191
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
Q60803
Organism: Mus musculus/domesticus
Length: 567  
Fragment?: false
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Protein
P39429
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q61382
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
P70196
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
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Protein
Q3U8L1
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q3UHJ1
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
Q3UMS9
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
Q8C6X9
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q8CAQ7
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q3UHM2
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
Q3TWR1
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q9QXA1
Organism: Mus musculus/domesticus
Length: 311  
Fragment?: false
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Protein
Q3UDK1
Organism: Mus musculus/domesticus
Length: 580  
Fragment?: false
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Protein
D3YWU1
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
D3Z343
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
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Protein
Q8BJL1
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
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Protein
P62932
Organism: Mus musculus/domesticus
Length: 710  
Fragment?: false
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Protein
A0A2R8VI70
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
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Protein
Q5DTZ7
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: true
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Protein
H3BIV6
Organism: Mus musculus/domesticus
Length: 412  
Fragment?: false
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Protein
Q3KN92
Organism: Mus musculus/domesticus
Length: 710  
Fragment?: false
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Protein
H3BJD9
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: true
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Protein
Q69ZS0
Organism: Mus musculus/domesticus
Length: 1063  
Fragment?: false
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Protein
Q9CQ29
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: false
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Protein
Q922B6
Organism: Mus musculus/domesticus
Length: 594  
Fragment?: false
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Protein
F8WJF7
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
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Protein
A0A3Q4EGR0
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Publication
12665246 | -
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
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Publication
17210253 | -
First Author: Gamsjaeger R
Year: 2007
Journal: Trends Biochem Sci
Title: Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume: 32
Issue: 2
Pages: 63-70
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Publication
15963892 | -
First Author: Hall TM
Year: 2005
Journal: Curr Opin Struct Biol
Title: Multiple modes of RNA recognition by zinc finger proteins.
Volume: 15
Issue: 3
Pages: 367-73
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Publication
15718139 | -
First Author: Brown RS
Year: 2005
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: getting a grip on RNA.
Volume: 15
Issue: 1
Pages: 94-8
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Publication
10529348 | -
First Author: Klug A
Year: 1999
Journal: J Mol Biol
Title: Zinc finger peptides for the regulation of gene expression.
Volume: 293
Issue: 2
Pages: 215-8
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Publication
11179890 | -
First Author: Laity JH
Year: 2001
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: new insights into structural and functional diversity.
Volume: 11
Issue: 1
Pages: 39-46
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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