InterPro : 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 are stable 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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

9 Found In

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

0 Parent Features

10 Publications

First Author Title Year Journal Volume Pages
Matthews JM Zinc fingers--folds for many occasions. 2002 IUBMB Life 54 351-5
Gamsjaeger R Sticky fingers: zinc-fingers as protein-recognition motifs. 2007 Trends Biochem Sci 32 63-70
Hall TM Multiple modes of RNA recognition by zinc finger proteins. 2005 Curr Opin Struct Biol 15 367-73
Brown RS Zinc finger proteins: getting a grip on RNA. 2005 Curr Opin Struct Biol 15 94-8
Klug A Zinc finger peptides for the regulation of gene expression. 1999 J Mol Biol 293 215-8
Laity JH Zinc finger proteins: new insights into structural and functional diversity. 2001 Curr Opin Struct Biol 11 39-46
Borden KL The RING finger domain: a recent example of a sequence-structure family. 1996 Curr Opin Struct Biol 6 395-401
Lorick KL RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. 1999 Proc Natl Acad Sci U S A 96 11364-9
Borden KL The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. 1995 EMBO J 14 1532-41
Yokouchi M Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. 1999 J Biol Chem 274 31707-12

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)