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Protein Domain : IPR017907

Name  Zinc finger, RING-type, conserved site Short Name  Znf_RING_CS
Type  Conserved_site 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 arestable structures, and they rarely undergo conformational changes upon binding their target. A number of eukaryotic and viral proteins contain a conserved cysteine-rich domain of 40 to 60 residues (called C3HC4 zinc-finger or 'RING' finger) []that binds two atoms of zinc. There are two different variants, the C3HC4-type and the C3H2C3-type, which is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as "RING-H2 finger". The 3D structure []of the zinc ligation system is referred to as the "cross-brace" motif. This atypical conformation is also shared by the FYVE (see ) and PHD (see ) domains. Many proteins containing a RING finger play a key role in the ubiquitination pathway. The ubiquitination pathway generally involves three types of enzyme, know as E1, E2 and E3. E1 and E2 are ubiquitin conjugating enzymes. E1 acts first and passes ubiquitin to E2. E3 are ubiquitin protein ligases, responsible for substrate recognition. It has been shown [, ]that several RING fingers act as E3 enzymes in the ubiquitination process.More information about these proteins can be found at Protein of the Month: Zinc Fingers [].

Publication Counts Displayer

0 Child Features

0 Contains

1 Cross References

Source . Name

Subject . Primary Identifier
PS00518 PROSITE IPR017907

2 Data Sets

Name URL
Swiss-Prot data set
InterPro data set  

9 Found In

DB identifier Name Short Name Type
IPR001841 Zinc finger, RING-type Znf_RING Domain
IPR013083 Zinc finger, RING/FYVE/PHD-type Znf_RING/FYVE/PHD Domain
IPR012227 TNF receptor-associated factor TRAF TNF_rcpt--assoc_TRAF Family
IPR018957 Zinc finger, C3HC4 RING-type Znf_C3HC4_RING-type Domain
IPR004575 Cdk-activating kinase assembly factor MAT1/Tfb3 MAT1/Tfb3 Family
IPR011364 Breast cancer type 1 susceptibility protein (BRCA1) BRCA1 Family
IPR004580 DNA repair protein, Rad18 Rad18 Family
IPR016398 E3 ubiquitin-protein ligase p28 E3_ubiquitin-prot_ligase_p28 Family
IPR017335 E3 ubiquitin ligase, RNF8 E3_Ub_ligase_RNF8 Family

0 GO Annotation

0 Ontology Annotations

0 Parent Features

925 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0073753 Q9VY20 Drosophila melanogaster
FBpp0075181 Q9VV48 Drosophila melanogaster
FBpp0086906 P25172 Drosophila melanogaster
FBpp0078288 Q8I0J6 Drosophila melanogaster
FBpp0078287 Q9VNJ0 Drosophila melanogaster
FBpp0085754 Q9V8P9 Drosophila melanogaster
FBpp0076341 O46034 Drosophila melanogaster
FBpp0076342 Q9VSK2 Drosophila melanogaster
FBpp0071688 O76924 Drosophila melanogaster
FBpp0071563 Q9W2M0 Drosophila melanogaster
FBpp0070464 O76908 Drosophila melanogaster
FBpp0084614 Q9VB08 Drosophila melanogaster
FBpp0291240 Q9VJB0 Drosophila melanogaster
FBpp0075071 Q9VV77 Drosophila melanogaster
FBpp0074856 Q9VVS2 Drosophila melanogaster
FBpp0083244 Q9VDP8 Drosophila melanogaster
FBpp0072709 Q9W0D8 Drosophila melanogaster
FBpp0078038 Q9VP20 Drosophila melanogaster
FBpp0072626 Q9W0D7 Drosophila melanogaster
FBpp0086838 Q4QPY0 Drosophila melanogaster
FBpp0087350 Q7KPG8 Drosophila melanogaster
FBpp0077260 P50534 Drosophila melanogaster
FBpp0082202 Q9VFY3 Drosophila melanogaster
FBpp0086911 P35820 Drosophila melanogaster
FBpp0074730 Q9VW25 Drosophila melanogaster
FBpp0075392 Q8IQM1 Drosophila melanogaster
FBpp0076706 Q9VRV2 Drosophila melanogaster
FBpp0073752 Q9VY21 Drosophila melanogaster
FBpp0074479 Q9VWI4 Drosophila melanogaster
FBpp0073970 Q9VXP1 Drosophila melanogaster