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Search results 801 to 900 out of 901 for Traf6

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein Domain
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 in clusters, 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 the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1 , a ubiquitin-likeprotein in Xenopus laevis []. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.Certain stress-associated proteins (SAP) contain AN1 domain, often in combination with A20 zinc finger domains (SAP8) or C2H2 domains (SAP16) []. For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. The interact of Znf216 with IKK-gamma and RIP is mediated by the A20 zinc-finger domain, while its interaction with TRAF6 is mediated by the AN1 zinc-finger domain; therefore, both zinc-finger domains are involved in regulating the immune response []. The AN1 zinc finger domain is also found in proteins containing a ubiquitin-like domain, which are involved in the ubiquitination pathway []. Proteins containing an AN1-type zinc finger include:Ascidian posterior end mark 6 (pem-6) protein [].Human AWP1 protein (associated with PRK1), which is expressed during early embryogenesis [].Human immunoglobulin mu binding protein 2 (SMUBP-2), mutations in which cause muscular atrophy with respiratory distress type 1 [].
Protein Domain
Type: Homologous_superfamily
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 in clusters, 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 the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1 , a ubiquitin-likeprotein in Xenopus laevis []. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.Certain stress-associated proteins (SAP) contain AN1 domain, often in combination with A20 zinc finger domains (SAP8) or C2H2 domains (SAP16) []. For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. The interact of Znf216 with IKK-gamma and RIP is mediated by the A20 zinc-finger domain, while its interaction with TRAF6 is mediated by the AN1 zinc-finger domain; therefore, both zinc-finger domains are involved in regulating the immune response []. The AN1 zinc finger domain is also found in proteins containing a ubiquitin-like domain, which are involved in the ubiquitination pathway []. Proteins containing an AN1-type zinc finger include:Ascidian posterior end mark 6 (pem-6) protein [].Human AWP1 protein (associated with PRK1), which is expressed during early embryogenesis [].Human immunoglobulin mu binding protein 2 (SMUBP-2), mutations in which cause muscular atrophy with respiratory distress type 1 [].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 601  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
Publication
First Author: Duan W
Year: 2000
Journal: Gene
Title: Cloning and characterization of AWP1, a novel protein that associates with serine/threonine kinase PRK1 in vivo.
Volume: 256
Issue: 1-2
Pages: 113-21
Publication
First Author: Huang J
Year: 2004
Journal: J Biol Chem
Title: ZNF216 Is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation.
Volume: 279
Issue: 16
Pages: 16847-53
Protein
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
Publication
First Author: Linnen JM
Year: 1993
Journal: Gene
Title: Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins.
Volume: 128
Issue: 2
Pages: 181-8
Publication
First Author: Satou Y
Year: 1997
Journal: Dev Biol
Title: Posterior end mark 2 (pem-2), pem-4, pem-5, and pem-6: maternal genes with localized mRNA in the ascidian embryo.
Volume: 192
Issue: 2
Pages: 467-81
Publication
First Author: Vij S
Year: 2006
Journal: Mol Genet Genomics
Title: Genome-wide analysis of the stress associated protein (SAP) gene family containing A20/AN1 zinc-finger(s) in rice and their phylogenetic relationship with Arabidopsis.
Volume: 276
Issue: 6
Pages: 565-75
Publication
First Author: Yang M
Year: 2019
Journal: Dig Dis Sci
Title: Effects and Mechanism of Constitutive TL1A Expression on Intestinal Mucosal Barrier in DSS-Induced Colitis.
Volume: 64
Issue: 7
Pages: 1844-1856
Publication
First Author: Kanazawa K
Year: 2005
Journal: J Bone Miner Res
Title: Self-assembled RANK induces osteoclastogenesis ligand-independently.
Volume: 20
Issue: 11
Pages: 2053-60
Publication
First Author: Wang L
Year: 2021
Journal: mBio
Title: The Ubiquitin Sensor and Adaptor Protein p62 Mediates Signal Transduction of a Viral Oncogenic Pathway.
Volume: 12
Issue: 5
Pages: e0109721
Protein
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 951  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 934  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 951  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 934  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: true
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 567  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 758  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1008  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1739  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1642  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1733  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1800  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1714  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1794  
Fragment?: false
Publication
First Author: Meroni G
Year: 2005
Journal: Bioessays
Title: TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases.
Volume: 27
Issue: 11
Pages: 1147-57
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 993  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 993  
Fragment?: false
Publication
First Author: Liepinsh E
Year: 2003
Journal: J Mol Biol
Title: Solution structure of the R3H domain from human Smubp-2.
Volume: 326
Issue: 1
Pages: 217-23
Protein
Organism: Mus musculus/domesticus
Length: 832  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 471  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1020  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1035  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 525  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1035  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 989  
Fragment?: true
Publication
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
Publication
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
Publication
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
Publication
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
Publication
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