InterPro : IPR001841

Name  Zinc finger, RING-type Short Name  Znf_RING
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 RING-type zinc finger domains. The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc, and is probably involved in mediating protein-protein interactions [, , ]. There are two different variants, the C3HC4-type and a C3H2C3-type, which are clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as 'RING-H2 finger'. The RING domain is a protein interaction domain that has been implicated in a range of diverse biological processes. E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain. E3 ubiquitin-protein ligases determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently, however, U-box proteins, which contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans, have been identified as a new type of E3 []. Various RING fingers also exhibit binding to E2 ubiquitin-conjugating enzymes (Ubc's) [, , ].Several 3D-structures for RING-fingers are known [, ]. The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the 'cross-brace' motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion, whilst pairs two and four bind the second.Note that in the older literature, some RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family, albeit with similar Cys-spacing (see ).

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR024766 Zinc finger, RING-H2-type Znf_RING_H2 Domain
IPR027934 Cellulose synthase, RING-type zinc finger CES_Znf_RING Domain

1 Contains

Id Name Short Name Type
IPR017907 Zinc finger, RING-type, conserved site Znf_RING_CS Conserved_site

18 Found In

Id Name Short Name Type
IPR004162 E3 ubiquitin-protein ligase SINA like SINA_like Family
IPR016528 Vacuolar protein sorting-associated protein 11 VPS11 Family
IPR017375 Peroxisome assembly protein 12 PEX12 Family
IPR004575 Cdk-activating kinase assemblyfactor MAT1/Tfb3 MAT1/Tfb3 Family
IPR016818 Nitric oxide synthase-interacting Nitric_oxide_synth-interacting Family
IPR011364 Breast cancer type 1 susceptibility protein (BRCA1) BRCA1 Family
IPR015459 Ubiquitin-protein ligase E3 MDM2 MDM2_E3_ligase Family
IPR004580 DNA repair protein, Rad18 Rad18 Family
IPR016902 Vacuolar protein sorting-associated protein 41 VPS41 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
IPR016495 p53 negative regulator Mdm2/Mdm4 p53_neg-reg_MDM_2/4 Family
IPR016569 Methyltransferase, trithorax MeTrfase_trithorax Family
IPR015458 MDM4 MDM4 Family
IPR001237 43kDa postsynaptic protein Postsynaptic Family
IPR017066 S-ribonuclease binding protein, SBP1, pollen S-RNase-bd_SBP1_pollen Family
IPR007954 Baculovirus immediate-early Baculo_IE-1 Family

1 Parent Features

Id Name Short Name Type
IPR013083 Zinc finger, RING/FYVE/PHD-type Znf_RING/FYVE/PHD Domain

13 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
Freemont PS The RING finger. A novel protein sequence motif related to the zinc finger. 1993 Ann N Y Acad Sci 684 174-92
Saurin AJ Does this have a familiar RING? 1996 Trends Biochem Sci 21 208-14
Freemont PS RING for destruction? 2000 Curr Biol 10 R84-7
Barinaga M A new finger on the protein destruction button. 1999 Science 286 223, 225
Joazeiro CA The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. 1999 Science 286 309-12
Hatakeyama S Ubiquitylation as a quality control system for intracellular proteins. 2003 J Biochem 134 1-8

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)