Summary: A20-like zinc finger
A20-like zinc finger Provide feedback
The A20 Zn-finger of bovine/human Rabex5/rabGEF1 is a Ubiquitin Binding Domain [5-6]. The zinc finger mediates self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.
De Valck D, Heyninck K, Van Criekinge W, Contreras R, Beyaert R, Fiers W; , FEBS Lett 1996;384:61-64.: A20, an inhibitor of cell death, self-associates by its zinc finger domain. PUBMED:8797804 EPMC:8797804
Song HY, Rothe M, Goeddel DV; , Proc Natl Acad Sci U S A 1996;93:6721-6725.: The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation. PUBMED:8692885 EPMC:8692885
Penengo L, Mapelli M, Murachelli AG, Confalonieri S, Magri L, Musacchio A, Di Fiore PP, Polo S, Schneider TR;, Cell. 2006;124:1183-1195.: Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. PUBMED:16499958 EPMC:16499958
Lee S, Tsai YC, Mattera R, Smith WJ, Kostelansky MS, Weissman AM, Bonifacino JS, Hurley JH;, Nat Struct Mol Biol. 2006;13:264-271.: Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5. PUBMED:16462746 EPMC:16462746
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002653
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 [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. 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 [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents the zinc finger domain found in A20. A20 is an inhibitor of cell death that inhibits NF-kappaB activation via the tumour necrosis factor receptor associated factor pathway [PUBMED:17449604]. The zinc finger domains appear to mediate self-association in A20. These fingers also mediate IL-1-induced NF-kappa B activation.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||DNA binding (GO:0003677)|
|zinc ion binding (GO:0008270)|
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Curation and family details
|Number in seed:||141|
|Number in full:||2002|
|Average length of the domain:||23.90 aa|
|Average identity of full alignment:||46 %|
|Average coverage of the sequence by the domain:||8.70 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the zf-A20 domain has been found. There are 24 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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